Magnesium in PDB 7qjt: Crystal Structure of A Cutinase Enzyme From Thermobifida Cellulosilytica TB100 (711)
Protein crystallography data
The structure of Crystal Structure of A Cutinase Enzyme From Thermobifida Cellulosilytica TB100 (711), PDB code: 7qjt
was solved by
M.Zahn,
T.J.Shakespeare,
G.T.Beckham,
J.E.Mcgeehan,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
77.29 /
1.78
|
Space group
|
P 43 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
109.297,
109.297,
44.184,
90,
90,
90
|
R / Rfree (%)
|
18.2 /
24.2
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of A Cutinase Enzyme From Thermobifida Cellulosilytica TB100 (711)
(pdb code 7qjt). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the
Crystal Structure of A Cutinase Enzyme From Thermobifida Cellulosilytica TB100 (711), PDB code: 7qjt:
Jump to Magnesium binding site number:
1;
2;
3;
Magnesium binding site 1 out
of 3 in 7qjt
Go back to
Magnesium Binding Sites List in 7qjt
Magnesium binding site 1 out
of 3 in the Crystal Structure of A Cutinase Enzyme From Thermobifida Cellulosilytica TB100 (711)
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 A Cutinase Enzyme From Thermobifida Cellulosilytica TB100 (711) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg303
b:2.1
occ:1.00
|
HE2
|
A:HIS267
|
1.0
|
34.9
|
0.0
|
HE2
|
A:HIS265
|
1.1
|
23.4
|
0.0
|
H2
|
A:ALA1
|
1.2
|
18.9
|
1.0
|
NE2
|
A:HIS267
|
1.8
|
32.7
|
1.0
|
NE2
|
A:HIS265
|
1.9
|
22.6
|
1.0
|
O
|
A:ALA1
|
1.9
|
18.0
|
1.0
|
N
|
A:ALA1
|
2.1
|
19.8
|
1.0
|
H3
|
A:ALA1
|
2.5
|
19.4
|
1.0
|
H1
|
A:ALA1
|
2.6
|
19.4
|
1.0
|
CE1
|
A:HIS267
|
2.8
|
31.4
|
1.0
|
CD2
|
A:HIS267
|
2.8
|
32.9
|
1.0
|
C
|
A:ALA1
|
2.9
|
18.6
|
1.0
|
CE1
|
A:HIS265
|
2.9
|
22.4
|
1.0
|
CD2
|
A:HIS265
|
2.9
|
23.1
|
1.0
|
HD2
|
A:HIS267
|
3.1
|
32.6
|
1.0
|
HE1
|
A:HIS267
|
3.1
|
31.8
|
1.0
|
CA
|
A:ALA1
|
3.1
|
18.7
|
1.0
|
HE1
|
A:HIS265
|
3.1
|
22.2
|
1.0
|
HD2
|
A:HIS265
|
3.1
|
23.4
|
1.0
|
HA
|
A:ALA1
|
3.7
|
18.8
|
1.0
|
HD3
|
A:PRO3
|
3.8
|
20.4
|
1.0
|
ND1
|
A:HIS267
|
3.9
|
32.1
|
1.0
|
ND1
|
A:HIS265
|
3.9
|
22.5
|
1.0
|
CG
|
A:HIS267
|
4.0
|
32.6
|
1.0
|
HB3
|
A:ALA1
|
4.0
|
18.6
|
1.0
|
CG
|
A:HIS265
|
4.0
|
23.4
|
1.0
|
N
|
A:ASN2
|
4.1
|
18.3
|
1.0
|
CB
|
A:ALA1
|
4.1
|
18.5
|
1.0
|
O
|
A:HOH515
|
4.4
|
34.4
|
1.0
|
HA
|
A:ASN2
|
4.6
|
19.1
|
1.0
|
HB2
|
A:ALA1
|
4.6
|
18.7
|
1.0
|
O
|
A:HOH578
|
4.7
|
24.1
|
1.0
|
CD
|
A:PRO3
|
4.7
|
20.2
|
1.0
|
HD1
|
A:HIS267
|
4.7
|
33.9
|
0.0
|
HB3
|
A:PRO3
|
4.8
|
20.6
|
1.0
|
HD1
|
A:HIS265
|
4.8
|
23.4
|
0.0
|
H
|
A:ASN2
|
4.8
|
18.6
|
1.0
|
HB1
|
A:ALA1
|
4.8
|
18.4
|
1.0
|
CA
|
A:ASN2
|
4.8
|
19.3
|
1.0
|
N
|
A:PRO3
|
4.9
|
20.0
|
1.0
|
|
Magnesium binding site 2 out
of 3 in 7qjt
Go back to
Magnesium Binding Sites List in 7qjt
Magnesium binding site 2 out
of 3 in the Crystal Structure of A Cutinase Enzyme From Thermobifida Cellulosilytica TB100 (711)
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 A Cutinase Enzyme From Thermobifida Cellulosilytica TB100 (711) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg304
b:23.1
occ:1.00
|
O
|
A:HOH475
|
1.9
|
21.1
|
1.0
|
OE1
|
A:GLU201
|
2.0
|
19.5
|
1.0
|
O
|
A:HOH414
|
2.0
|
20.2
|
1.0
|
OE2
|
A:GLU185
|
2.1
|
16.7
|
1.0
|
OE2
|
A:GLU253
|
2.1
|
17.4
|
1.0
|
O
|
A:HOH444
|
2.1
|
23.4
|
1.0
|
CD
|
A:GLU201
|
3.0
|
19.9
|
1.0
|
CD
|
A:GLU185
|
3.2
|
17.6
|
1.0
|
CD
|
A:GLU253
|
3.2
|
17.5
|
1.0
|
HG2
|
A:GLU253
|
3.2
|
17.5
|
1.0
|
OE2
|
A:GLU201
|
3.3
|
21.9
|
1.0
|
HE2
|
A:TYR199
|
3.6
|
16.8
|
1.0
|
HH21
|
A:ARG255
|
3.6
|
20.1
|
1.0
|
OE1
|
A:GLU185
|
3.7
|
17.8
|
1.0
|
CG
|
A:GLU253
|
3.7
|
17.3
|
1.0
|
HG22
|
A:VAL180
|
3.8
|
14.5
|
1.0
|
O
|
A:HOH540
|
3.9
|
36.3
|
1.0
|
HG23
|
A:VAL180
|
4.0
|
14.6
|
1.0
|
OH
|
A:TYR199
|
4.1
|
17.4
|
1.0
|
HG3
|
A:GLU253
|
4.1
|
17.3
|
1.0
|
OE1
|
A:GLU253
|
4.3
|
17.8
|
1.0
|
HB2
|
A:GLU201
|
4.3
|
18.4
|
1.0
|
NH2
|
A:ARG255
|
4.3
|
20.4
|
1.0
|
O
|
A:HOH615
|
4.3
|
45.0
|
1.0
|
CG
|
A:GLU201
|
4.3
|
18.9
|
1.0
|
CG2
|
A:VAL180
|
4.4
|
14.5
|
1.0
|
CE2
|
A:TYR199
|
4.4
|
16.6
|
1.0
|
HG2
|
A:GLU252
|
4.4
|
27.1
|
1.0
|
HH22
|
A:ARG255
|
4.5
|
20.1
|
1.0
|
CG
|
A:GLU185
|
4.5
|
17.4
|
1.0
|
HG2
|
A:GLU185
|
4.5
|
17.3
|
1.0
|
HG3
|
A:GLU252
|
4.6
|
27.1
|
1.0
|
HB3
|
A:GLU201
|
4.6
|
18.5
|
1.0
|
CB
|
A:GLU201
|
4.7
|
18.4
|
1.0
|
HG3
|
A:GLU185
|
4.7
|
17.3
|
1.0
|
HH
|
A:TYR199
|
4.7
|
17.6
|
0.0
|
CZ
|
A:TYR199
|
4.8
|
16.8
|
1.0
|
HG3
|
A:GLU201
|
4.8
|
18.9
|
1.0
|
HG2
|
A:GLU201
|
5.0
|
19.1
|
1.0
|
HB3
|
A:GLU253
|
5.0
|
18.3
|
1.0
|
HG21
|
A:VAL180
|
5.0
|
14.6
|
1.0
|
CG
|
A:GLU252
|
5.0
|
27.3
|
1.0
|
|
Magnesium binding site 3 out
of 3 in 7qjt
Go back to
Magnesium Binding Sites List in 7qjt
Magnesium binding site 3 out
of 3 in the Crystal Structure of A Cutinase Enzyme From Thermobifida Cellulosilytica TB100 (711)
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 A Cutinase Enzyme From Thermobifida Cellulosilytica TB100 (711) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg305
b:38.3
occ:1.00
|
OD1
|
A:ASN203
|
1.9
|
35.1
|
1.0
|
OE1
|
A:GLU252
|
2.0
|
32.8
|
1.0
|
O
|
A:HOH497
|
2.4
|
41.4
|
1.0
|
O
|
A:HOH526
|
2.5
|
37.0
|
1.0
|
OE1
|
A:GLU173
|
2.6
|
29.3
|
1.0
|
OE2
|
A:GLU173
|
3.0
|
33.4
|
1.0
|
CD
|
A:GLU252
|
3.0
|
29.2
|
1.0
|
CG
|
A:ASN203
|
3.0
|
34.0
|
1.0
|
CD
|
A:GLU173
|
3.1
|
28.3
|
1.0
|
HD21
|
A:ASN203
|
3.3
|
35.4
|
1.0
|
HB2
|
A:GLU252
|
3.5
|
24.7
|
1.0
|
OE2
|
A:GLU252
|
3.6
|
31.6
|
1.0
|
ND2
|
A:ASN203
|
3.6
|
35.8
|
1.0
|
HA
|
A:ASN203
|
3.8
|
25.6
|
1.0
|
CG
|
A:GLU252
|
4.0
|
27.3
|
1.0
|
HA
|
A:GLU252
|
4.1
|
22.1
|
1.0
|
H
|
A:GLY204
|
4.1
|
24.9
|
1.0
|
CB
|
A:GLU252
|
4.2
|
25.1
|
1.0
|
HG2
|
A:GLU252
|
4.3
|
27.1
|
1.0
|
CB
|
A:ASN203
|
4.3
|
29.0
|
1.0
|
HD22
|
A:ASN203
|
4.5
|
35.2
|
1.0
|
CA
|
A:ASN203
|
4.5
|
25.6
|
1.0
|
CG
|
A:GLU173
|
4.6
|
25.3
|
1.0
|
CA
|
A:GLU252
|
4.7
|
21.6
|
1.0
|
N
|
A:GLY204
|
4.7
|
25.3
|
1.0
|
HB3
|
A:ASN203
|
4.8
|
29.3
|
1.0
|
HG3
|
A:GLU252
|
4.9
|
27.1
|
1.0
|
HG3
|
A:GLU173
|
4.9
|
25.5
|
1.0
|
HB2
|
A:GLU173
|
4.9
|
23.4
|
1.0
|
HB2
|
A:ASN203
|
4.9
|
29.1
|
1.0
|
|
Reference:
E.Erickson,
J.E.Gado,
L.Avilan,
F.Bratti,
R.K.Brizendine,
P.A.Cox,
R.Gill,
R.Graham,
D.J.Kim,
G.Konig,
W.E.Michener,
S.Poudel,
K.J.Ramirez,
T.J.Shakespeare,
M.Zahn,
E.S.Boyd,
C.M.Payne,
J.L.Dubois,
A.R.Pickford,
G.T.Beckham,
J.E.Mcgeehan.
Sourcing Thermotolerant Poly(Ethylene Terephthalate) Hydrolase Scaffolds From Natural Diversity Nat Commun V. 13 7850 2022.
ISSN: ESSN 2041-1723
DOI: 10.1038/S41467-022-35237-X
Page generated: Thu Oct 3 05:09:38 2024
|