Magnesium in PDB 5t3r: Crystal Structure of BT1762-1763
Protein crystallography data
The structure of Crystal Structure of BT1762-1763, PDB code: 5t3r
was solved by
B.Van Den Berg,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
75.89 /
3.10
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
151.770,
117.330,
119.890,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.7 /
25.9
|
Other elements in 5t3r:
The structure of Crystal Structure of BT1762-1763 also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of BT1762-1763
(pdb code 5t3r). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the
Crystal Structure of BT1762-1763, PDB code: 5t3r:
Jump to Magnesium binding site number:
1;
2;
Magnesium binding site 1 out
of 2 in 5t3r
Go back to
Magnesium Binding Sites List in 5t3r
Magnesium binding site 1 out
of 2 in the Crystal Structure of BT1762-1763
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 BT1762-1763 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg601
b:53.3
occ:1.00
|
O
|
A:TYR273
|
1.9
|
56.6
|
1.0
|
OD1
|
D:ASN664
|
1.9
|
85.3
|
1.0
|
OD1
|
A:ASN401
|
2.3
|
77.1
|
1.0
|
OE2
|
A:GLU262
|
2.5
|
45.7
|
1.0
|
OE1
|
A:GLU262
|
2.6
|
62.1
|
1.0
|
O
|
A:SER399
|
2.8
|
56.9
|
1.0
|
CD
|
A:GLU262
|
2.9
|
58.0
|
1.0
|
C
|
A:TYR273
|
3.1
|
41.9
|
1.0
|
CG
|
D:ASN664
|
3.1
|
65.4
|
1.0
|
CG
|
A:ASN401
|
3.4
|
64.4
|
1.0
|
N
|
A:TYR273
|
3.6
|
51.8
|
1.0
|
CA
|
A:TYR273
|
3.9
|
49.6
|
1.0
|
C
|
A:SER399
|
3.9
|
54.1
|
1.0
|
ND2
|
D:ASN664
|
4.0
|
65.3
|
1.0
|
C
|
A:GLN272
|
4.0
|
52.8
|
1.0
|
N
|
A:SER274
|
4.1
|
47.7
|
1.0
|
ND2
|
A:ASN401
|
4.1
|
75.7
|
1.0
|
CA
|
D:ASN664
|
4.2
|
60.1
|
1.0
|
CB
|
D:ASN664
|
4.2
|
53.2
|
1.0
|
N
|
A:ASN401
|
4.2
|
55.7
|
1.0
|
CB
|
A:SER399
|
4.3
|
68.9
|
1.0
|
CA
|
A:GLN272
|
4.3
|
54.9
|
1.0
|
CG
|
A:GLU262
|
4.4
|
53.7
|
1.0
|
OE1
|
A:GLN272
|
4.4
|
62.6
|
1.0
|
CA
|
A:SER274
|
4.4
|
43.3
|
1.0
|
CB
|
A:TYR273
|
4.4
|
60.2
|
1.0
|
CB
|
A:ASN401
|
4.5
|
47.8
|
1.0
|
OG
|
A:SER399
|
4.5
|
68.0
|
1.0
|
CA
|
A:ASN401
|
4.5
|
53.9
|
1.0
|
CA
|
A:SER399
|
4.6
|
62.7
|
1.0
|
C
|
A:LEU400
|
4.7
|
63.1
|
1.0
|
N
|
D:ASN664
|
4.7
|
57.3
|
1.0
|
O
|
A:GLN272
|
4.7
|
55.8
|
1.0
|
OD2
|
D:ASP659
|
4.9
|
66.3
|
1.0
|
CB
|
A:GLN272
|
4.9
|
50.6
|
1.0
|
N
|
A:LEU400
|
4.9
|
45.4
|
1.0
|
CB
|
A:SER274
|
5.0
|
40.8
|
1.0
|
|
Magnesium binding site 2 out
of 2 in 5t3r
Go back to
Magnesium Binding Sites List in 5t3r
Magnesium binding site 2 out
of 2 in the Crystal Structure of BT1762-1763
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 BT1762-1763 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg1101
b:45.7
occ:1.00
|
O
|
D:VAL843
|
1.7
|
68.7
|
1.0
|
OD1
|
D:ASP848
|
1.7
|
67.4
|
1.0
|
OD1
|
D:ASP837
|
2.3
|
64.9
|
1.0
|
OD2
|
D:ASP839
|
2.3
|
69.1
|
1.0
|
OD1
|
D:ASN841
|
2.4
|
53.9
|
1.0
|
CB
|
D:ASP839
|
2.7
|
51.6
|
1.0
|
CG
|
D:ASP848
|
2.8
|
66.9
|
1.0
|
CG
|
D:ASP839
|
2.8
|
60.5
|
1.0
|
C
|
D:VAL843
|
2.9
|
50.5
|
1.0
|
OD2
|
D:ASP848
|
3.2
|
61.0
|
1.0
|
CG
|
D:ASN841
|
3.4
|
53.0
|
1.0
|
CG
|
D:ASP837
|
3.5
|
58.4
|
1.0
|
CA
|
D:ILE844
|
3.7
|
64.6
|
1.0
|
N
|
D:ILE844
|
3.7
|
54.1
|
1.0
|
OD1
|
D:ASP845
|
3.8
|
89.5
|
1.0
|
ND2
|
D:ASN841
|
3.8
|
64.0
|
1.0
|
C
|
D:ILE844
|
3.9
|
73.2
|
1.0
|
O
|
D:ILE844
|
3.9
|
73.7
|
1.0
|
N
|
D:VAL843
|
4.0
|
73.6
|
1.0
|
CA
|
D:VAL843
|
4.0
|
56.7
|
1.0
|
OD1
|
D:ASP839
|
4.0
|
68.4
|
1.0
|
OD2
|
D:ASP837
|
4.0
|
51.6
|
1.0
|
CA
|
D:ASP839
|
4.1
|
51.7
|
1.0
|
CB
|
D:ASP848
|
4.1
|
74.3
|
1.0
|
CG2
|
D:VAL843
|
4.2
|
52.4
|
1.0
|
N
|
D:ASP839
|
4.3
|
60.0
|
1.0
|
CG
|
D:ASP845
|
4.4
|
80.2
|
1.0
|
OD2
|
D:ASP845
|
4.4
|
80.8
|
1.0
|
CB
|
D:ASP837
|
4.6
|
52.8
|
1.0
|
N
|
D:ASP845
|
4.6
|
70.7
|
1.0
|
CB
|
D:VAL843
|
4.6
|
51.7
|
1.0
|
CB
|
D:ASN841
|
4.6
|
54.0
|
1.0
|
N
|
D:ASN841
|
4.6
|
53.3
|
1.0
|
N
|
D:GLY842
|
4.7
|
57.9
|
1.0
|
CA
|
D:ASP837
|
4.7
|
50.4
|
1.0
|
C
|
D:ASP839
|
4.9
|
74.0
|
1.0
|
N
|
D:HIS840
|
4.9
|
73.1
|
1.0
|
C
|
D:ASN841
|
4.9
|
57.4
|
1.0
|
CA
|
D:ASN841
|
5.0
|
54.0
|
1.0
|
|
Reference:
A.J.Glenwright,
K.R.Pothula,
S.P.Bhamidimarri,
D.S.Chorev,
A.Basle,
S.J.Firbank,
H.Zheng,
C.V.Robinson,
M.Winterhalter,
U.Kleinekathofer,
D.N.Bolam,
B.Van Den Berg.
Structural Basis For Nutrient Acquisition By Dominant Members of the Human Gut Microbiota. Nature V. 541 407 2017.
ISSN: ESSN 1476-4687
PubMed: 28077872
DOI: 10.1038/NATURE20828
Page generated: Mon Dec 14 21:11:11 2020
|