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Magnesium in PDB 6s83: Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp

Enzymatic activity of Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp

All present enzymatic activity of Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp:
2.5.1.6;

Protein crystallography data

The structure of Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp, PDB code: 6s83 was solved by M.Degano, C.Minici, M.Porcelli, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 74.47 / 2.34
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 78.196, 111.430, 400.400, 90.00, 90.00, 90.00
R / Rfree (%) 20.7 / 24

Magnesium Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 21;

Binding sites:

The binding sites of Magnesium atom in the Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp (pdb code 6s83). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 21 binding sites of Magnesium where determined in the Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp, PDB code: 6s83:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Magnesium binding site 1 out of 21 in 6s83

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Magnesium binding site 1 out of 21 in the Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:40.2
occ:1.00
O1 B:PO4501 1.9 52.7 1.0
O6 A:MDN501 2.0 46.7 1.0
OD2 A:ASP32 2.1 52.7 1.0
O A:HOH625 2.1 44.1 1.0
O A:HOH607 2.2 47.4 1.0
O2 A:MDN501 2.3 55.1 1.0
CG A:ASP32 3.1 44.6 1.0
P B:PO4501 3.1 67.7 1.0
P5 A:MDN501 3.1 48.8 1.0
HZ1 A:LYS26 3.2 61.1 1.0
O4 B:PO4501 3.3 66.8 1.0
P1 A:MDN501 3.3 53.4 1.0
HE1 A:HIS30 3.4 47.4 1.0
OD1 A:ASP32 3.4 45.6 1.0
HZ3 A:LYS26 3.5 61.1 1.0
C4 A:MDN501 3.5 50.0 1.0
O A:HOH612 3.5 40.5 1.0
HH21 A:ARG286 3.7 60.4 1.0
HB3 A:ARG286 3.7 57.7 1.0
H41 A:MDN501 3.8 60.0 1.0
NZ A:LYS26 3.8 51.0 1.0
O7 A:MDN501 3.8 42.4 1.0
O3 A:MDN501 3.9 44.5 1.0
O2 B:PO4501 4.0 66.4 1.0
HE A:ARG286 4.0 59.8 1.0
HE2 A:LYS26 4.1 59.9 1.0
NH2 A:ARG286 4.1 50.3 1.0
O3 B:PO4501 4.2 67.4 1.0
MG B:MG502 4.2 42.3 1.0
CE1 A:HIS30 4.3 39.5 1.0
O8 A:MDN501 4.4 49.1 1.0
H42 A:MDN501 4.4 60.0 1.0
CB A:ASP32 4.4 38.4 1.0
HB2 A:ARG286 4.4 57.7 1.0
NE A:ARG286 4.4 49.9 1.0
MG B:MG503 4.5 49.3 1.0
HB2 A:ASP32 4.5 46.0 1.0
HZ2 A:LYS26 4.5 61.1 1.0
CB A:ARG286 4.5 48.1 1.0
O A:ASP281 4.5 48.5 1.0
CZ A:ARG286 4.5 50.4 1.0
CE A:LYS26 4.5 49.9 1.0
HH22 A:ARG286 4.5 60.4 1.0
O1 A:MDN501 4.6 56.3 1.0
HE2 A:HIS30 4.7 47.6 1.0
HA2 A:GLY282 4.7 55.7 1.0
O A:ARG286 4.8 49.0 1.0
OE1 B:GLN64 4.8 58.2 1.0
HZ2 B:LYS308 4.8 64.8 1.0
HB3 A:ASP32 4.9 46.0 1.0
HG3 A:ARG286 4.9 58.8 1.0
NE2 A:HIS30 4.9 39.7 1.0
OD1 A:ASP280 4.9 69.7 1.0
H A:ASP32 5.0 49.9 1.0

Magnesium binding site 2 out of 21 in 6s83

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Magnesium binding site 2 out of 21 in the Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg504

b:58.3
occ:1.00
OD2 A:ASP159 2.1 83.2 1.0
O B:HOH634 2.2 56.6 1.0
O B:HOH657 2.2 61.0 1.0
O B:HOH621 2.2 60.6 1.0
O2A B:ACP504 2.3 76.9 1.0
CG A:ASP159 3.1 80.3 1.0
PA B:ACP504 3.5 75.5 1.0
HB3 A:ASP159 3.6 93.6 1.0
O3A B:ACP504 3.6 76.0 1.0
CB A:ASP159 3.9 78.0 1.0
O1B B:ACP504 3.9 75.3 1.0
OD1 A:ASP159 4.0 81.0 1.0
OD1 A:ASN158 4.1 83.9 1.0
HD21 A:ASN158 4.2 97.9 1.0
HB2 A:ASP159 4.2 93.6 1.0
PB B:ACP504 4.3 75.0 1.0
O1A B:ACP504 4.6 77.8 1.0
O5' B:ACP504 4.6 77.3 1.0
O2B B:ACP504 4.7 75.0 1.0
CG A:ASN158 4.7 82.3 1.0
ND2 A:ASN158 4.7 81.6 1.0

Magnesium binding site 3 out of 21 in 6s83

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Magnesium binding site 3 out of 21 in the Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg502

b:42.3
occ:1.00
OE1 B:GLU303 2.1 54.5 1.0
O7 A:MDN501 2.1 42.4 1.0
OE2 B:GLU303 2.1 55.6 1.0
O3 A:MDN501 2.2 44.5 1.0
O B:HOH626 2.2 38.1 1.0
O4 B:PO4501 2.2 66.8 1.0
CD B:GLU303 2.3 49.5 1.0
H42 A:MDN501 2.9 60.0 1.0
P5 A:MDN501 3.0 48.8 1.0
C4 A:MDN501 3.0 50.0 1.0
HG B:SER161 3.0 58.6 1.0
P1 A:MDN501 3.0 53.4 1.0
HE1 B:HIS313 3.3 48.5 1.0
P B:PO4501 3.3 67.7 1.0
O2 B:PO4501 3.4 66.4 1.0
O B:HOH602 3.7 38.5 1.0
OG B:SER161 3.7 48.9 1.0
HZ1 A:LYS26 3.7 61.1 1.0
CG B:GLU303 3.8 42.8 1.0
O6 A:MDN501 3.9 46.7 1.0
H41 A:MDN501 3.9 60.0 1.0
OD2 B:ASP159 3.9 58.1 1.0
HE2 B:LYS308 4.0 61.5 1.0
O2 A:MDN501 4.0 55.1 1.0
O1 B:PO4501 4.0 52.7 1.0
CE1 B:HIS313 4.1 40.4 1.0
HA B:GLU303 4.1 48.2 1.0
HE2 B:HIS313 4.2 50.2 1.0
O8 A:MDN501 4.2 49.1 1.0
HG2 B:GLU303 4.2 51.4 1.0
HB3 B:SER161 4.2 59.7 1.0
O1 A:MDN501 4.2 56.3 1.0
MG A:MG502 4.2 40.2 1.0
HG3 B:GLU303 4.3 51.4 1.0
HB3 B:GLU303 4.4 45.8 1.0
CB B:SER161 4.5 49.7 1.0
NE2 B:HIS313 4.5 41.8 1.0
HE3 B:LYS308 4.5 61.5 1.0
O3 B:PO4501 4.5 67.4 1.0
CB B:GLU303 4.6 38.2 1.0
NZ A:LYS26 4.6 51.0 1.0
CE B:LYS308 4.7 51.3 1.0
HA3 B:GLY315 4.7 76.3 1.0
HZ3 A:LYS200 4.7 60.1 1.0
HZ2 B:LYS308 4.7 64.8 1.0
HE3 A:LYS26 4.8 59.9 1.0
HB2 B:SER161 4.8 59.7 1.0
CA B:GLU303 4.8 40.2 1.0
HZ2 A:LYS26 4.9 61.1 1.0
H5'1 A:SAM503 5.0 1.0 1.0

Magnesium binding site 4 out of 21 in 6s83

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Magnesium binding site 4 out of 21 in the Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg503

b:49.3
occ:1.00
OD2 B:ASP63 2.0 57.8 1.0
O A:HOH612 2.1 40.5 1.0
OE1 B:GLN64 2.2 58.2 1.0
OD1 B:ASP63 2.3 56.6 1.0
O B:HOH636 2.3 48.7 1.0
O A:HOH603 2.4 56.1 1.0
CG B:ASP63 2.4 53.3 1.0
O2 A:MDN501 2.7 55.1 1.0
HH22 A:ARG286 3.0 60.4 1.0
CD B:GLN64 3.3 54.5 1.0
O1 A:MDN501 3.4 56.3 1.0
HG2 B:GLN64 3.5 61.1 1.0
NH2 A:ARG286 3.6 50.3 1.0
HH21 A:ARG286 3.6 60.4 1.0
P1 A:MDN501 3.6 53.4 1.0
CG B:GLN64 3.9 51.0 1.0
CB B:ASP63 3.9 48.7 1.0
O A:HOH607 3.9 47.4 1.0
HG3 B:GLN64 4.1 61.1 1.0
HB2 A:ASP281 4.1 66.7 1.0
HE3 B:LYS308 4.1 61.5 1.0
HZ2 B:LYS308 4.2 64.8 1.0
HZ3 B:LYS308 4.2 64.8 1.0
O B:ASP63 4.2 41.1 1.0
HB2 B:ASP63 4.2 58.4 1.0
HN2 A:SAM503 4.2 0.4 1.0
HB3 B:ASN61 4.3 66.3 1.0
HN1 A:SAM503 4.3 0.4 1.0
H B:ASP63 4.3 54.9 1.0
O A:HOH625 4.4 44.1 1.0
HB3 B:ASP63 4.4 58.4 1.0
NE2 B:GLN64 4.4 52.2 1.0
MG A:MG502 4.5 40.2 1.0
H A:ASP281 4.5 70.0 1.0
C B:ASP63 4.5 41.0 1.0
NZ B:LYS308 4.5 54.0 1.0
O3 A:MDN501 4.5 44.5 1.0
OD1 A:ASP280 4.6 69.7 1.0
HE22 B:GLN64 4.6 62.7 1.0
O1 B:PO4501 4.6 52.7 1.0
O A:ASP281 4.6 48.5 1.0
CZ A:ARG286 4.7 50.4 1.0
N A:SAM503 4.7 89.5 1.0
CA B:ASP63 4.7 42.3 1.0
HE2 B:HIS313 4.7 50.2 1.0
HH12 A:ARG286 4.7 62.2 1.0
HG2 B:LYS308 4.8 57.3 1.0
CE B:LYS308 4.8 51.3 1.0
N B:ASP63 4.9 45.8 1.0
H41 A:MDN501 4.9 60.0 1.0

Magnesium binding site 5 out of 21 in 6s83

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Magnesium binding site 5 out of 21 in the Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg506

b:41.9
occ:1.00
O3G B:ACP504 2.0 50.5 1.0
O1 B:PO4505 2.0 48.0 1.0
OD2 B:ASP32 2.1 48.3 1.0
O B:HOH611 2.1 41.9 1.0
O B:HOH642 2.1 40.4 1.0
O B:HOH614 2.2 38.3 1.0
CG B:ASP32 2.9 40.8 1.0
OD1 B:ASP32 3.1 40.8 1.0
P B:PO4505 3.2 50.6 1.0
HE1 B:HIS30 3.2 47.0 1.0
PG B:ACP504 3.4 60.0 1.0
HZ1 B:LYS26 3.5 50.2 1.0
O3 B:PO4505 3.5 47.7 1.0
H3B2 B:ACP504 3.6 80.5 1.0
HB3 B:ARG286 3.6 52.2 1.0
O4 B:PO4505 3.7 50.6 1.0
HH21 B:ARG286 3.7 54.5 1.0
HZ3 B:LYS26 3.7 50.2 1.0
HE B:ARG286 3.9 53.6 1.0
HE2 B:LYS26 3.9 47.4 1.0
C3B B:ACP504 3.9 67.1 1.0
NZ B:LYS26 4.0 41.8 1.0
H3B1 B:ACP504 4.1 80.5 1.0
CE1 B:HIS30 4.1 39.2 1.0
NH2 B:ARG286 4.1 45.4 1.0
O B:HOH651 4.2 48.8 1.0
O1G B:ACP504 4.3 60.9 1.0
O2G B:ACP504 4.3 58.0 1.0
CB B:ASP32 4.3 35.4 1.0
NE B:ARG286 4.3 44.7 1.0
O B:ASP281 4.4 41.1 1.0
HB2 B:ARG286 4.4 52.2 1.0
O2 B:PO4505 4.4 52.0 1.0
CB B:ARG286 4.4 43.5 1.0
HA2 B:GLY282 4.5 45.3 1.0
HB2 B:ASP32 4.5 42.5 1.0
CE B:LYS26 4.5 39.5 1.0
CZ B:ARG286 4.5 44.9 1.0
OE1 A:GLN64 4.5 39.5 1.0
HH22 B:ARG286 4.6 54.5 1.0
HE2 B:HIS30 4.7 47.2 1.0
O B:ARG286 4.7 44.1 1.0
HZ2 B:LYS26 4.7 50.2 1.0
HB3 B:ASP32 4.8 42.5 1.0
HZ1 A:LYS308 4.8 49.9 1.0
HG3 B:ARG286 4.8 51.2 1.0
H B:ASP32 4.8 44.7 1.0
NE2 B:HIS30 4.8 39.4 1.0
HE3 B:LYS26 5.0 47.4 1.0

Magnesium binding site 6 out of 21 in 6s83

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Magnesium binding site 6 out of 21 in the Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg507

b:75.0
occ:1.00
O2B B:ACP504 2.1 75.0 1.0
O B:HOH603 2.1 74.4 1.0
O B:HOH619 2.2 75.3 1.0
O B:HOH647 2.2 70.0 1.0
O B:HOH632 2.2 57.9 1.0
O1G B:ACP504 2.2 60.9 1.0
HZ2 B:LYS200 3.4 78.1 1.0
PB B:ACP504 3.5 75.0 1.0
PG B:ACP504 3.6 60.0 1.0
OE2 B:GLU24 3.6 76.0 1.0
HE3 B:LYS26 3.7 47.4 1.0
O4 B:PO4505 3.8 50.6 1.0
C3B B:ACP504 4.0 67.1 1.0
OE1 B:GLU24 4.1 75.7 1.0
HZ1 B:LYS26 4.1 50.2 1.0
H3B2 B:ACP504 4.2 80.5 1.0
NZ B:LYS200 4.2 65.1 1.0
CD B:GLU24 4.3 74.2 1.0
HE2 B:LYS200 4.3 75.8 1.0
HZ3 B:LYS200 4.3 78.1 1.0
O3A B:ACP504 4.3 76.0 1.0
OE2 A:GLU303 4.3 66.9 1.0
O2G B:ACP504 4.4 58.0 1.0
HD3 B:LYS200 4.5 76.3 1.0
O1B B:ACP504 4.5 75.3 1.0
HG3 A:GLU303 4.5 73.2 1.0
CE B:LYS26 4.5 39.5 1.0
O3G B:ACP504 4.6 50.5 1.0
NZ B:LYS26 4.6 41.8 1.0
HZ2 B:LYS26 4.7 50.2 1.0
CE B:LYS200 4.7 63.2 1.0
HE2 B:LYS26 4.8 47.4 1.0
HZ1 B:LYS200 4.9 78.1 1.0
H3B1 B:ACP504 4.9 80.5 1.0
O3 B:PO4505 5.0 47.7 1.0

Magnesium binding site 7 out of 21 in 6s83

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Magnesium binding site 7 out of 21 in the Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg503

b:50.8
occ:1.00
O4 C:PO4502 1.9 57.9 1.0
OD2 C:ASP32 2.1 60.2 1.0
O2 C:MDN501 2.1 53.4 1.0
O8 C:MDN501 2.1 55.3 1.0
O C:HOH606 2.2 51.0 1.0
O C:HOH618 2.2 45.4 1.0
CG C:ASP32 3.0 49.5 1.0
P5 C:MDN501 3.2 55.8 1.0
HE1 C:HIS30 3.2 50.6 1.0
OD1 C:ASP32 3.3 49.9 1.0
P1 C:MDN501 3.3 54.0 1.0
P C:PO4502 3.3 66.4 1.0
C4 C:MDN501 3.5 53.6 1.0
HZ1 C:LYS26 3.5 62.1 1.0
O1 C:PO4502 3.6 66.6 1.0
O6 C:MDN501 3.7 47.9 1.0
H42 C:MDN501 3.7 64.3 1.0
HZ3 C:LYS26 3.8 62.1 1.0
HH21 C:ARG286 3.8 55.9 1.0
HB3 C:ARG286 3.9 57.5 1.0
HE2 C:LYS26 4.0 59.3 1.0
NZ C:LYS26 4.0 51.8 1.0
O1 C:MDN501 4.0 48.5 1.0
O C:HOH634 4.0 42.3 1.0
O2 C:PO4502 4.1 67.5 1.0
CE1 C:HIS30 4.2 42.2 1.0
MG D:MG502 4.2 39.5 1.0
HE C:ARG286 4.2 59.9 1.0
MG D:MG501 4.2 46.7 1.0
NH2 C:ARG286 4.2 46.6 1.0
O C:HOH655 4.3 51.7 1.0
O3 C:PO4502 4.3 66.0 1.0
O C:ASP281 4.4 43.3 1.0
CB C:ASP32 4.4 44.8 1.0
H41 C:MDN501 4.4 64.3 1.0
HB2 C:ASP32 4.4 53.7 1.0
HA2 C:GLY282 4.5 50.0 1.0
O3 C:MDN501 4.5 53.0 1.0
O7 C:MDN501 4.6 57.4 1.0
CE C:LYS26 4.6 49.4 1.0
NE C:ARG286 4.6 49.9 1.0
HH22 C:ARG286 4.6 55.9 1.0
HB2 C:ARG286 4.6 57.5 1.0
CZ C:ARG286 4.7 46.8 1.0
CB C:ARG286 4.7 47.9 1.0
HE2 C:HIS30 4.8 51.5 1.0
HZ1 D:LYS308 4.8 73.3 1.0
HZ2 C:LYS26 4.8 62.1 1.0
H C:ASP32 4.9 46.3 1.0
HB3 C:ASP32 4.9 53.7 1.0
NE2 C:HIS30 4.9 42.9 1.0
OE1 D:GLN64 4.9 50.4 1.0
O C:ARG286 5.0 42.7 1.0

Magnesium binding site 8 out of 21 in 6s83

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Magnesium binding site 8 out of 21 in the Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 8 of Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg501

b:46.7
occ:1.00
OE1 D:GLU303 2.0 62.4 1.0
OE2 D:GLU303 2.1 62.0 1.0
O6 C:MDN501 2.1 47.9 1.0
O1 C:MDN501 2.1 48.5 1.0
O D:HOH632 2.2 42.5 1.0
O1 C:PO4502 2.3 66.6 1.0
CD D:GLU303 2.3 56.0 1.0
P1 C:MDN501 3.2 54.0 1.0
HE1 D:HIS313 3.2 60.0 1.0
P5 C:MDN501 3.2 55.8 1.0
P C:PO4502 3.3 66.4 1.0
O2 C:PO4502 3.3 67.5 1.0
C4 C:MDN501 3.4 53.6 1.0
HG D:SER161 3.4 59.6 1.0
H41 C:MDN501 3.5 64.3 1.0
HE2 D:LYS308 3.6 69.8 1.0
HZ1 C:LYS26 3.6 62.1 1.0
O2 C:MDN501 3.7 53.4 1.0
CG D:GLU303 3.8 46.8 1.0
O4 C:PO4502 3.8 57.9 1.0
O C:HOH603 3.9 48.9 1.0
HA D:GLU303 3.9 49.3 1.0
O8 C:MDN501 4.0 55.3 1.0
CE1 D:HIS313 4.0 50.0 1.0
OG D:SER161 4.1 49.6 1.0
HG2 D:GLU303 4.1 56.2 1.0
HE2 D:HIS313 4.1 61.9 1.0
MG C:MG503 4.2 50.8 1.0
HB3 D:GLU303 4.3 50.3 1.0
HB3 D:SER161 4.3 54.8 1.0
H42 C:MDN501 4.3 64.3 1.0
HG3 D:GLU303 4.3 56.2 1.0
HZ1 D:LYS308 4.4 73.3 1.0
O7 C:MDN501 4.4 57.4 1.0
CE D:LYS308 4.4 58.2 1.0
NE2 D:HIS313 4.4 51.6 1.0
CB D:GLU303 4.5 41.9 1.0
NZ C:LYS26 4.5 51.8 1.0
OD2 D:ASP159 4.5 68.6 1.0
O3 C:MDN501 4.5 53.0 1.0
HE3 D:LYS308 4.5 69.8 1.0
O3 C:PO4502 4.6 66.0 1.0
HA3 D:GLY315 4.6 59.5 1.0
CA D:GLU303 4.7 41.1 1.0
CB D:SER161 4.7 45.7 1.0
HZ2 C:LYS26 4.8 62.1 1.0
HE3 C:LYS26 4.8 59.3 1.0
NZ D:LYS308 4.8 61.1 1.0
HZ3 C:LYS200 4.9 55.7 1.0
H D:ALA304 4.9 59.5 1.0
HZ3 C:LYS26 5.0 62.1 1.0

Magnesium binding site 9 out of 21 in 6s83

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Magnesium binding site 9 out of 21 in the Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 9 of Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg502

b:39.5
occ:1.00
OD2 D:ASP63 2.2 50.5 1.0
OE1 D:GLN64 2.2 50.4 1.0
O C:HOH634 2.3 42.3 1.0
O C:HOH601 2.3 51.9 1.0
O D:HOH647 2.3 42.8 1.0
O8 C:MDN501 2.6 55.3 1.0
CG D:ASP63 2.8 47.5 1.0
OD1 D:ASP63 2.8 49.6 1.0
HH22 C:ARG286 3.1 55.9 1.0
CD D:GLN64 3.4 49.7 1.0
O C:HOH606 3.5 51.0 1.0
O7 C:MDN501 3.5 57.4 1.0
NH2 C:ARG286 3.6 46.6 1.0
HG2 D:GLN64 3.6 57.2 1.0
HH21 C:ARG286 3.6 55.9 1.0
P5 C:MDN501 3.6 55.8 1.0
HB2 C:ASP281 3.7 54.0 1.0
CG D:GLN64 3.9 47.6 1.0
O C:HOH618 4.0 45.4 1.0
HG3 D:GLN64 4.1 57.2 1.0
O C:ASP281 4.1 43.3 1.0
MG C:MG503 4.2 50.8 1.0
CB D:ASP63 4.3 39.9 1.0
H C:ASP281 4.3 58.0 1.0
HE3 D:LYS308 4.4 69.8 1.0
HB2 D:ASP63 4.4 47.8 1.0
O D:ASP63 4.5 36.5 1.0
HZ1 D:LYS308 4.5 73.3 1.0
NE2 D:GLN64 4.5 49.4 1.0
O6 C:MDN501 4.6 47.9 1.0
CZ C:ARG286 4.6 46.8 1.0
HE22 D:GLN64 4.6 59.2 1.0
HB3 D:ASN61 4.6 68.1 1.0
HH12 C:ARG286 4.6 57.9 1.0
CB C:ASP281 4.7 45.0 1.0
HZ2 D:LYS308 4.7 73.3 1.0
O4 C:PO4502 4.7 57.9 1.0
C C:ASP281 4.7 44.8 1.0
H D:ASP63 4.8 49.9 1.0
C D:ASP63 4.8 40.0 1.0
HB3 D:ASP63 4.8 47.8 1.0
NZ D:LYS308 4.9 61.1 1.0
H42 C:MDN501 5.0 64.3 1.0
NH1 C:ARG286 5.0 48.2 1.0

Magnesium binding site 10 out of 21 in 6s83

Go back to Magnesium Binding Sites List in 6s83
Magnesium binding site 10 out of 21 in the Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 10 of Crystal Structure of Methionine Adenosyltransferase From Pyrococcus Furiosus in Complex with Amppcp, Sam, and Pcp within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg505

b:49.8
occ:1.00
O4 D:PO4504 2.0 57.1 1.0
O D:HOH619 2.0 44.8 1.0
O1G D:ACP503 2.1 53.9 1.0
OD2 D:ASP32 2.1 58.6 1.0
O D:HOH629 2.1 44.8 1.0
O D:HOH657 2.1 50.1 1.0
CG D:ASP32 3.0 49.5 1.0
OD1 D:ASP32 3.1 51.5 1.0
P D:PO4504 3.3 63.8 1.0
HE1 D:HIS30 3.4 46.5 1.0
PG D:ACP503 3.5 61.1 1.0
HH21 D:ARG286 3.5 43.5 1.0
HE22 C:GLN64 3.6 66.8 1.0
HZ1 D:LYS26 3.7 54.5 1.0
H3B1 D:ACP503 3.8 81.0 1.0
O3 D:PO4504 3.8 65.7 1.0
O1 D:PO4504 3.9 65.2 1.0
HB3 D:ARG286 3.9 46.8 1.0
HE D:ARG286 4.0 49.0 1.0
HZ3 D:LYS26 4.0 54.5 1.0
NH2 D:ARG286 4.0 36.2 1.0
C3B D:ACP503 4.0 67.5 1.0
O D:HOH652 4.0 46.1 1.0
O C:HOH646 4.1 60.6 1.0
H3B2 D:ACP503 4.1 81.0 1.0
O D:ASP281 4.2 44.9 1.0
HE21 C:GLN64 4.2 66.8 1.0
NZ D:LYS26 4.2 45.4 1.0
HE2 D:LYS26 4.2 51.3 1.0
NE2 C:GLN64 4.3 55.7 1.0
CE1 D:HIS30 4.3 38.7 1.0
O2G D:ACP503 4.3 61.0 1.0
HA2 D:GLY282 4.4 42.5 1.0
NE D:ARG286 4.4 40.8 1.0
CB D:ASP32 4.4 43.7 1.0
HH22 D:ARG286 4.4 43.5 1.0
O3G D:ACP503 4.4 55.8 1.0
CZ D:ARG286 4.4 40.2 1.0
HB2 D:ASP32 4.5 52.4 1.0
O2 D:PO4504 4.5 65.1 1.0
HB2 D:ARG286 4.6 46.8 1.0
HZ1 C:LYS308 4.6 52.5 1.0
CB D:ARG286 4.7 39.0 1.0
CE D:LYS26 4.8 42.8 1.0
H D:ASP32 4.8 45.9 1.0
HB3 D:ASP32 4.9 52.4 1.0
HG3 D:ARG286 4.9 48.4 1.0
HE2 D:HIS30 4.9 45.6 1.0
HZ2 D:LYS26 5.0 54.5 1.0

Reference:

C.Minici, L.Mosca, C.Paola Ilisso, G.Cacciapuoti, M.Porcelli, M.Degano. Structures of Catalytic Cycle Intermediates of the Pyrococcus Furiosus Methionine Adenosyltransferase Demonstrate Negative Cooperativity in the Archaeal Orthologues. J.Struct.Biol. 07462 2020.
ISSN: ESSN 1095-8657
PubMed: 31962159
DOI: 10.1016/J.JSB.2020.107462
Page generated: Tue Oct 1 17:48:35 2024

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