Copper in PDB 2ygi: Methanobactin HM1
Protein crystallography data
The structure of Methanobactin HM1, PDB code: 2ygi
was solved by
A.Ghazouani,
A.Basle,
S.J.Firbank,
J.Gray,
C.Dennison,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.00 /
0.80
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
9.072,
22.535,
23.572,
64.79,
86.06,
91.77
|
R / Rfree (%)
|
6.5 /
8.9
|
Copper Binding Sites:
The binding sites of Copper atom in the Methanobactin HM1
(pdb code 2ygi). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the
Methanobactin HM1, PDB code: 2ygi:
Jump to Copper binding site number:
1;
2;
3;
4;
Copper binding site 1 out
of 4 in 2ygi
Go back to
Copper Binding Sites List in 2ygi
Copper binding site 1 out
of 4 in the Methanobactin HM1
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Methanobactin HM1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu7
b:1.7
occ:1.00
|
NBA
|
A:HM84
|
2.1
|
1.5
|
1.0
|
NAB
|
A:HM71
|
2.1
|
1.5
|
1.0
|
SAE
|
A:HM71
|
2.2
|
2.0
|
1.0
|
SBG
|
A:HM84
|
2.3
|
1.9
|
1.0
|
CAB
|
A:HM84
|
2.9
|
1.4
|
1.0
|
CA
|
A:HM71
|
2.9
|
1.6
|
1.0
|
C
|
A:HM71
|
3.0
|
2.0
|
1.0
|
C
|
A:HM84
|
3.0
|
1.5
|
1.0
|
CAA
|
A:HM71
|
3.0
|
1.4
|
1.0
|
CAZ
|
A:HM84
|
3.2
|
1.6
|
1.0
|
CBR
|
A:HM71
|
3.2
|
1.8
|
1.0
|
N
|
A:HM84
|
3.8
|
1.6
|
1.0
|
CAA
|
A:HM84
|
3.8
|
1.5
|
1.0
|
CBS
|
A:HM71
|
3.9
|
2.4
|
1.0
|
CAV
|
A:HM84
|
4.1
|
1.8
|
1.0
|
O
|
B:HOH2006
|
4.2
|
5.6
|
1.0
|
CBC
|
A:HM84
|
4.2
|
1.7
|
1.0
|
N
|
A:ALA2
|
4.3
|
2.2
|
1.0
|
OBB
|
A:HM84
|
4.3
|
1.8
|
1.0
|
N
|
A:ALA5
|
4.3
|
1.7
|
1.0
|
CAF
|
A:HM71
|
4.3
|
1.5
|
1.0
|
CAI
|
A:HM71
|
4.4
|
1.8
|
1.0
|
SBT
|
A:HM71
|
4.7
|
2.1
|
0.6
|
CAW
|
A:HM84
|
4.7
|
2.2
|
1.0
|
O
|
A:HOH2004
|
4.8
|
9.1
|
1.0
|
NAH
|
A:HM71
|
4.8
|
1.8
|
1.0
|
CB
|
B:ALA6
|
4.8
|
6.1
|
1.0
|
N
|
A:SER3
|
4.9
|
2.2
|
1.0
|
|
Copper binding site 2 out
of 4 in 2ygi
Go back to
Copper Binding Sites List in 2ygi
Copper binding site 2 out
of 4 in the Methanobactin HM1
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Methanobactin HM1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu7
b:2.0
occ:1.00
|
NBA
|
B:HM84
|
2.1
|
2.0
|
1.0
|
NAB
|
B:HM71
|
2.1
|
2.0
|
1.0
|
SAE
|
B:HM71
|
2.3
|
2.4
|
1.0
|
SBG
|
B:HM84
|
2.3
|
1.8
|
1.0
|
CAB
|
B:HM84
|
2.9
|
1.9
|
1.0
|
CA
|
B:HM71
|
3.0
|
2.2
|
1.0
|
C
|
B:HM71
|
3.0
|
2.0
|
1.0
|
CAA
|
B:HM71
|
3.0
|
2.4
|
1.0
|
C
|
B:HM84
|
3.0
|
1.6
|
1.0
|
CAZ
|
B:HM84
|
3.2
|
1.6
|
1.0
|
CBR
|
B:HM71
|
3.2
|
2.6
|
1.0
|
N
|
B:HM84
|
3.7
|
2.0
|
1.0
|
CAA
|
B:HM84
|
3.8
|
2.0
|
1.0
|
CBS
|
B:HM71
|
3.8
|
2.6
|
1.0
|
CAV
|
B:HM84
|
4.0
|
2.6
|
1.0
|
O
|
D:HOH2002
|
4.1
|
6.0
|
1.0
|
CBC
|
B:HM84
|
4.2
|
1.5
|
1.0
|
OBB
|
B:HM84
|
4.3
|
1.9
|
1.0
|
N
|
B:ALA2
|
4.3
|
2.9
|
1.0
|
CAF
|
B:HM71
|
4.3
|
2.2
|
1.0
|
N
|
B:ALA5
|
4.3
|
1.9
|
1.0
|
CAI
|
B:HM71
|
4.4
|
2.6
|
1.0
|
O
|
B:HOH2002
|
4.6
|
6.6
|
1.0
|
CAW
|
B:HM84
|
4.6
|
3.5
|
1.0
|
CB
|
D:ALA6
|
4.7
|
6.9
|
1.0
|
SBT
|
B:HM71
|
4.8
|
2.7
|
1.0
|
NAH
|
B:HM71
|
4.8
|
2.4
|
1.0
|
N
|
B:SER3
|
4.9
|
2.5
|
1.0
|
C
|
B:SER3
|
5.0
|
2.1
|
1.0
|
|
Copper binding site 3 out
of 4 in 2ygi
Go back to
Copper Binding Sites List in 2ygi
Copper binding site 3 out
of 4 in the Methanobactin HM1
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Methanobactin HM1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu7
b:2.5
occ:1.00
|
NBA
|
C:HM84
|
2.1
|
2.0
|
1.0
|
NAB
|
C:HM71
|
2.1
|
2.7
|
1.0
|
SAE
|
C:HM71
|
2.3
|
3.1
|
1.0
|
SBG
|
C:HM84
|
2.3
|
2.5
|
1.0
|
CAB
|
C:HM84
|
2.9
|
2.2
|
1.0
|
CA
|
C:HM71
|
3.0
|
2.8
|
1.0
|
C
|
C:HM71
|
3.0
|
3.1
|
1.0
|
C
|
C:HM84
|
3.0
|
2.2
|
1.0
|
CAA
|
C:HM71
|
3.0
|
3.2
|
1.0
|
CAZ
|
C:HM84
|
3.2
|
5.0
|
1.0
|
CBR
|
C:HM71
|
3.2
|
3.5
|
1.0
|
N
|
C:HM84
|
3.7
|
2.7
|
1.0
|
CAA
|
C:HM84
|
3.8
|
2.8
|
1.0
|
CBS
|
C:HM71
|
3.8
|
4.0
|
1.0
|
CAV
|
C:HM84
|
3.9
|
3.7
|
1.0
|
CB
|
A:ALA6
|
4.0
|
2.0
|
0.2
|
CBC
|
C:HM84
|
4.2
|
2.6
|
1.0
|
OBB
|
C:HM84
|
4.3
|
2.8
|
1.0
|
N
|
C:ALA2
|
4.3
|
3.6
|
1.0
|
N
|
C:ALA5
|
4.3
|
2.4
|
1.0
|
CAF
|
C:HM71
|
4.3
|
3.0
|
1.0
|
CAI
|
C:HM71
|
4.4
|
3.0
|
1.0
|
O
|
A:HOH2009
|
4.4
|
6.2
|
1.0
|
CAW
|
C:HM84
|
4.6
|
4.2
|
1.0
|
CB
|
A:ALA6
|
4.6
|
12.3
|
0.8
|
O
|
A:HOH2010
|
4.7
|
6.2
|
1.0
|
SBT
|
C:HM71
|
4.7
|
3.3
|
1.0
|
NAH
|
C:HM71
|
4.8
|
3.0
|
1.0
|
N
|
C:SER3
|
4.9
|
3.0
|
1.0
|
C
|
C:SER3
|
4.9
|
3.3
|
1.0
|
C
|
C:ALA2
|
5.0
|
3.2
|
1.0
|
|
Copper binding site 4 out
of 4 in 2ygi
Go back to
Copper Binding Sites List in 2ygi
Copper binding site 4 out
of 4 in the Methanobactin HM1
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Methanobactin HM1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu7
b:1.7
occ:1.00
|
NBA
|
D:HM84
|
2.1
|
1.7
|
1.0
|
NAB
|
D:HM71
|
2.1
|
1.9
|
1.0
|
SAE
|
D:HM71
|
2.2
|
2.2
|
1.0
|
SBG
|
D:HM84
|
2.3
|
1.6
|
1.0
|
CAB
|
D:HM84
|
2.9
|
1.5
|
1.0
|
CA
|
D:HM71
|
2.9
|
1.8
|
1.0
|
C
|
D:HM71
|
3.0
|
2.1
|
1.0
|
C
|
D:HM84
|
3.0
|
1.3
|
1.0
|
CAA
|
D:HM71
|
3.0
|
1.6
|
1.0
|
CAZ
|
D:HM84
|
3.2
|
2.3
|
1.0
|
CBR
|
D:HM71
|
3.2
|
1.6
|
1.0
|
N
|
D:HM84
|
3.8
|
2.2
|
1.0
|
CBS
|
D:HM71
|
3.8
|
1.8
|
1.0
|
CAA
|
D:HM84
|
3.8
|
2.1
|
1.0
|
CAV
|
D:HM84
|
4.0
|
2.1
|
1.0
|
CBC
|
D:HM84
|
4.2
|
1.7
|
1.0
|
OBB
|
D:HM84
|
4.3
|
2.4
|
1.0
|
N
|
D:ALA2
|
4.3
|
3.1
|
1.0
|
N
|
D:ALA5
|
4.3
|
1.5
|
1.0
|
CAF
|
D:HM71
|
4.3
|
1.8
|
1.0
|
CAI
|
D:HM71
|
4.4
|
1.7
|
1.0
|
CAW
|
D:HM84
|
4.7
|
2.8
|
1.0
|
SBT
|
D:HM71
|
4.8
|
2.5
|
1.0
|
NAH
|
D:HM71
|
4.8
|
1.9
|
1.0
|
N
|
D:SER3
|
4.9
|
3.1
|
1.0
|
|
Reference:
A.El Ghazouani,
A.Basle,
J.Gray,
D.W.Graham,
S.J.Firbank,
C.Dennison.
Variations in Methanobactin Structure Influences Copper Utilization By Methane-Oxidizing Bacteria. Proc.Natl.Acad.Sci.Usa V. 109 8400 2012.
ISSN: ISSN 0027-8424
PubMed: 22582172
DOI: 10.1073/PNAS.1112921109
Page generated: Wed Jul 31 00:25:08 2024
|