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Magnesium in PDB 7uiy: Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia

Enzymatic activity of Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia

All present enzymatic activity of Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia:
3.4.21.92;

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia (pdb code 7uiy). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia, PDB code: 7uiy:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in 7uiy

Go back to Magnesium Binding Sites List in 7uiy
Magnesium binding site 1 out of 5 in the Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg803

b:74.0
occ:1.00
HG1 A:THR502 2.5 101.0 1.0
OG1 A:THR502 2.6 101.0 1.0
O3G A:AGS802 2.8 90.7 1.0
HG1 A:THR604 3.0 111.2 1.0
O2B A:AGS802 3.0 90.7 1.0
OG1 A:THR604 3.7 111.2 1.0
HH22 B:ARG643 3.8 54.0 1.0
CB A:THR502 3.9 101.0 1.0
HG3 A:LYS501 4.0 99.8 1.0
HD2 A:LYS501 4.0 99.8 1.0
HB3 A:ASP564 4.1 112.3 1.0
HG21 A:THR502 4.1 101.0 1.0
PG A:AGS802 4.2 90.7 1.0
HB A:THR502 4.2 101.0 1.0
HB A:THR604 4.2 111.2 1.0
OD1 A:ASP564 4.2 112.3 1.0
PB A:AGS802 4.3 90.7 1.0
HG21 A:THR604 4.4 111.2 1.0
CG A:ASP564 4.4 112.3 1.0
O3B A:AGS802 4.4 90.7 1.0
NH2 B:ARG643 4.5 54.0 1.0
HH21 B:ARG643 4.5 54.0 1.0
CB A:THR604 4.5 111.2 1.0
CG2 A:THR502 4.6 101.0 1.0
H A:THR502 4.7 101.0 1.0
OD1 A:ASN606 4.7 101.4 1.0
CG A:LYS501 4.7 99.8 1.0
CB A:ASP564 4.7 112.3 1.0
O2A A:AGS802 4.8 90.7 1.0
CD A:LYS501 4.8 99.8 1.0
HD22 A:ASN606 4.8 101.4 1.0
HG2 A:LYS501 4.9 99.8 1.0
O2G A:AGS802 4.9 90.7 1.0
HH21 A:ARG518 4.9 108.5 1.0
HA A:ASP564 4.9 112.3 1.0
OD2 A:ASP564 4.9 112.3 1.0
O3A A:AGS802 4.9 90.7 1.0
CG2 A:THR604 4.9 111.2 1.0
HG23 A:THR502 5.0 101.0 1.0
CA A:THR502 5.0 101.0 1.0

Magnesium binding site 2 out of 5 in 7uiy

Go back to Magnesium Binding Sites List in 7uiy
Magnesium binding site 2 out of 5 in the Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg803

b:41.1
occ:1.00
O2B B:AGS802 2.0 34.2 1.0
OG1 B:THR502 2.1 35.3 1.0
HG1 B:THR604 2.8 37.8 1.0
OD2 B:ASP564 3.0 39.6 1.0
OD1 B:ASP564 3.2 39.6 1.0
PB B:AGS802 3.2 34.2 1.0
CG B:ASP564 3.4 39.6 1.0
S1G B:AGS802 3.4 34.2 1.0
CB B:THR502 3.4 35.3 1.0
OG1 B:THR604 3.5 37.8 1.0
HB B:THR502 3.6 35.3 1.0
O1B B:AGS802 3.7 34.2 1.0
H B:THR502 3.9 35.3 1.0
HB B:THR604 3.9 37.8 1.0
HB2 B:LYS501 3.9 37.2 1.0
HG21 B:THR502 3.9 35.3 1.0
O3B B:AGS802 4.0 34.2 1.0
HH22 C:ARG643 4.0 29.5 1.0
HG21 B:THR604 4.0 37.8 1.0
OE1 B:GLU565 4.1 39.0 1.0
HD21 B:ASN606 4.1 36.9 1.0
CB B:THR604 4.2 37.8 1.0
N B:THR502 4.2 35.3 1.0
PG B:AGS802 4.2 34.2 1.0
CG2 B:THR502 4.3 35.3 1.0
HE3 B:LYS501 4.3 37.2 1.0
CA B:THR502 4.3 35.3 1.0
O3A B:AGS802 4.4 34.2 1.0
HA B:THR502 4.5 35.3 1.0
O2G B:AGS802 4.5 34.2 1.0
CG2 B:THR604 4.6 37.8 1.0
NH2 C:ARG643 4.7 29.5 1.0
HB3 B:LYS501 4.7 37.2 1.0
CB B:LYS501 4.7 37.2 1.0
CB B:ASP564 4.7 39.6 1.0
HG23 B:THR502 4.8 35.3 1.0
HH21 C:ARG643 4.8 29.5 1.0
O2A B:AGS802 4.8 34.2 1.0
HB2 B:ASP564 4.8 39.6 1.0
ND2 B:ASN606 4.9 36.9 1.0
HG23 B:THR604 4.9 37.8 1.0
HG22 B:THR502 5.0 35.3 1.0

Magnesium binding site 3 out of 5 in 7uiy

Go back to Magnesium Binding Sites List in 7uiy
Magnesium binding site 3 out of 5 in the Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg804

b:49.7
occ:1.00
OG1 B:THR221 2.0 55.7 1.0
O1B B:AGS801 2.0 52.9 1.0
O2B B:AGS801 2.4 52.9 1.0
PB B:AGS801 2.6 52.9 1.0
HB B:THR221 2.6 55.7 1.0
HG21 B:THR221 2.7 55.7 1.0
CB B:THR221 2.7 55.7 1.0
HH22 C:ARG340 3.1 42.2 1.0
CG2 B:THR221 3.2 55.7 1.0
NH2 C:ARG340 3.7 42.2 1.0
HG22 B:THR221 3.7 55.7 1.0
O5' B:AGS801 3.7 52.9 1.0
O3A B:AGS801 3.7 52.9 1.0
HH21 C:ARG340 3.8 42.2 1.0
OD1 B:ASP285 3.8 61.4 1.0
O3B B:AGS801 3.9 52.9 1.0
HG23 B:THR221 3.9 55.7 1.0
H B:THR221 4.1 55.7 1.0
CA B:THR221 4.1 55.7 1.0
OD2 B:ASP285 4.2 61.4 1.0
O2A B:AGS801 4.2 52.9 1.0
PA B:AGS801 4.2 52.9 1.0
CG B:ASP285 4.3 61.4 1.0
O3G B:AGS801 4.4 52.9 1.0
HA B:THR221 4.5 55.7 1.0
PG B:AGS801 4.5 52.9 1.0
N B:THR221 4.5 55.7 1.0
S1G B:AGS801 4.5 52.9 1.0
H5'1 B:AGS801 4.6 52.9 1.0
HG3 B:LYS220 4.7 57.2 1.0
C5' B:AGS801 4.7 52.9 1.0
HH12 C:ARG340 4.8 42.2 1.0
CZ C:ARG340 4.8 42.2 1.0
HH21 C:ARG339 4.9 43.6 1.0
H5'2 B:AGS801 4.9 52.9 1.0

Magnesium binding site 4 out of 5 in 7uiy

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Magnesium binding site 4 out of 5 in the Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg803

b:39.5
occ:1.00
HG23 C:THR502 1.9 30.2 1.0
HG21 C:THR502 2.0 30.2 1.0
CG2 C:THR502 2.3 30.2 1.0
S1G C:AGS802 2.4 28.7 1.0
HG22 C:THR502 2.9 30.2 1.0
O3B C:AGS802 3.0 28.7 1.0
PG C:AGS802 3.1 28.7 1.0
HG1 C:THR502 3.2 30.2 1.0
O2B C:AGS802 3.3 28.7 1.0
HH22 D:ARG643 3.3 34.9 1.0
O2A C:AGS802 3.5 28.7 1.0
O3G C:AGS802 3.5 28.7 1.0
CB C:THR502 3.5 30.2 1.0
OG1 C:THR502 3.6 30.2 1.0
PB C:AGS802 3.7 28.7 1.0
HH22 C:ARG702 3.8 35.7 1.0
OD1 C:ASP564 4.0 34.6 1.0
NH2 D:ARG643 4.0 34.9 1.0
H C:THR502 4.0 30.2 1.0
HB C:THR502 4.0 30.2 1.0
HH21 D:ARG643 4.1 34.9 1.0
HG1 C:THR604 4.2 31.5 1.0
O3A C:AGS802 4.4 28.7 1.0
PA C:AGS802 4.4 28.7 1.0
HB2 C:LYS501 4.5 32.5 1.0
HE3 C:LYS501 4.5 32.5 1.0
O2G C:AGS802 4.5 28.7 1.0
N C:THR502 4.5 30.2 1.0
NH2 C:ARG702 4.6 35.7 1.0
CA C:THR502 4.7 30.2 1.0
OE1 C:GLU565 4.7 37.3 1.0
OD2 D:ASP582 4.7 36.5 1.0
CG C:ASP564 4.7 34.6 1.0
O1A C:AGS802 4.8 28.7 1.0
HH21 C:ARG702 4.9 35.7 1.0
OG1 C:THR604 4.9 31.5 1.0
HH12 D:ARG643 5.0 34.9 1.0

Magnesium binding site 5 out of 5 in 7uiy

Go back to Magnesium Binding Sites List in 7uiy
Magnesium binding site 5 out of 5 in the Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg803

b:48.3
occ:1.00
HG21 D:THR221 1.8 33.8 1.0
O3B D:AGS801 2.1 33.0 1.0
O2B D:AGS801 2.4 33.0 1.0
PB D:AGS801 2.4 33.0 1.0
O3A D:AGS801 2.4 33.0 1.0
CG2 D:THR221 2.7 33.8 1.0
HG22 D:THR221 2.9 33.8 1.0
PG D:AGS801 3.1 33.0 1.0
HG23 D:THR221 3.1 33.8 1.0
S1G D:AGS801 3.1 33.0 1.0
HH22 E:ARG339 3.1 33.2 1.0
HH22 E:ARG340 3.3 34.1 1.0
O3G D:AGS801 3.7 33.0 1.0
PA D:AGS801 3.8 33.0 1.0
OG1 D:THR221 3.8 33.8 1.0
HG1 D:THR221 3.8 33.8 1.0
H D:THR221 3.8 33.8 1.0
NH2 E:ARG339 3.8 33.2 1.0
CB D:THR221 3.9 33.8 1.0
O1B D:AGS801 3.9 33.0 1.0
NH2 E:ARG340 4.0 34.1 1.0
O5' D:AGS801 4.1 33.0 1.0
O2A D:AGS801 4.1 33.0 1.0
HH12 E:ARG340 4.1 34.1 1.0
HH21 E:ARG339 4.1 33.2 1.0
OD2 D:ASP285 4.3 38.0 1.0
O2G D:AGS801 4.3 33.0 1.0
HH21 E:ARG340 4.5 34.1 1.0
HB D:THR221 4.5 33.8 1.0
HH12 E:ARG339 4.5 33.2 1.0
N D:THR221 4.6 33.8 1.0
HB2 D:LYS220 4.6 31.8 1.0
HZ3 D:LYS220 4.7 31.8 1.0
NH1 E:ARG340 4.7 34.1 1.0
OD1 D:ASP285 4.8 38.0 1.0
CZ E:ARG340 4.8 34.1 1.0
CA D:THR221 4.9 33.8 1.0
CZ E:ARG339 4.9 33.2 1.0
HE2 D:LYS220 4.9 31.8 1.0
O1A D:AGS801 4.9 33.0 1.0
CG D:ASP285 5.0 38.0 1.0

Reference:

S.Kim, X.Fei, R.T.Sauer, T.A.Baker. Aaa+ Protease-Adaptor Structures Reveal Altered Conformations and Ring Specialization. Nat.Struct.Mol.Biol. V. 29 1068 2022.
ISSN: ESSN 1545-9985
PubMed: 36329286
DOI: 10.1038/S41594-022-00850-3
Page generated: Thu Oct 3 10:01:54 2024

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