Copper in PDB 2fwl: The Cytochrome C552/Cua Complex From Thermus Thermophilus
Enzymatic activity of The Cytochrome C552/Cua Complex From Thermus Thermophilus
All present enzymatic activity of The Cytochrome C552/Cua Complex From Thermus Thermophilus:
1.9.3.1;
Other elements in 2fwl:
The structure of The Cytochrome C552/Cua Complex From Thermus Thermophilus also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the The Cytochrome C552/Cua Complex From Thermus Thermophilus
(pdb code 2fwl). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the
The Cytochrome C552/Cua Complex From Thermus Thermophilus, PDB code: 2fwl:
Jump to Copper binding site number:
1;
2;
Copper binding site 1 out
of 2 in 2fwl
Go back to
Copper Binding Sites List in 2fwl
Copper binding site 1 out
of 2 in the The Cytochrome C552/Cua Complex From Thermus Thermophilus
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of The Cytochrome C552/Cua Complex From Thermus Thermophilus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu169
b:0.0
occ:1.00
|
CU1
|
B:CUA169
|
0.0
|
0.0
|
1.0
|
O
|
B:GLN151
|
1.8
|
0.0
|
1.0
|
ND1
|
B:HIS157
|
2.1
|
0.0
|
1.0
|
SG
|
B:CYS149
|
2.3
|
0.0
|
1.0
|
CU2
|
B:CUA169
|
2.4
|
0.0
|
1.0
|
SG
|
B:CYS153
|
2.5
|
0.0
|
1.0
|
CE1
|
B:HIS157
|
2.9
|
0.0
|
1.0
|
O
|
B:CYS149
|
2.9
|
0.0
|
1.0
|
C
|
B:GLN151
|
3.0
|
0.0
|
1.0
|
HE1
|
B:HIS157
|
3.0
|
0.0
|
1.0
|
HB3
|
B:CYS149
|
3.1
|
0.0
|
1.0
|
CG
|
B:HIS157
|
3.3
|
0.0
|
1.0
|
CB
|
B:CYS149
|
3.3
|
0.0
|
1.0
|
HB2
|
B:HIS157
|
3.4
|
0.0
|
1.0
|
HA
|
B:TYR152
|
3.6
|
0.0
|
1.0
|
O
|
B:TYR152
|
3.6
|
0.0
|
1.0
|
C
|
B:TYR152
|
3.6
|
0.0
|
1.0
|
C
|
B:CYS149
|
3.7
|
0.0
|
1.0
|
CB
|
B:HIS157
|
3.8
|
0.0
|
1.0
|
O
|
B:HIS157
|
3.8
|
0.0
|
1.0
|
N
|
B:TYR152
|
3.9
|
0.0
|
1.0
|
CB
|
B:CYS153
|
3.9
|
0.0
|
1.0
|
HB3
|
B:CYS153
|
3.9
|
0.0
|
1.0
|
HA
|
B:HIS114
|
3.9
|
0.0
|
1.0
|
CA
|
B:TYR152
|
3.9
|
0.0
|
1.0
|
HA
|
B:HIS157
|
3.9
|
0.0
|
1.0
|
HB3
|
B:MET160
|
4.0
|
0.0
|
1.0
|
N
|
B:CYS153
|
4.1
|
0.0
|
1.0
|
CA
|
B:GLN151
|
4.1
|
0.0
|
1.0
|
N
|
B:GLN151
|
4.1
|
0.0
|
1.0
|
NE2
|
B:HIS157
|
4.1
|
0.0
|
1.0
|
HB2
|
B:CYS149
|
4.2
|
0.0
|
1.0
|
CA
|
B:CYS149
|
4.2
|
0.0
|
1.0
|
CA
|
B:HIS157
|
4.3
|
0.0
|
1.0
|
H
|
B:GLN151
|
4.3
|
0.0
|
1.0
|
HB3
|
B:GLN151
|
4.3
|
0.0
|
1.0
|
CD2
|
B:HIS157
|
4.3
|
0.0
|
1.0
|
SD
|
B:MET160
|
4.3
|
0.0
|
1.0
|
ND1
|
B:HIS114
|
4.4
|
0.0
|
1.0
|
C
|
B:HIS157
|
4.4
|
0.0
|
1.0
|
C
|
B:ASN150
|
4.4
|
0.0
|
1.0
|
H
|
B:CYS153
|
4.5
|
0.0
|
1.0
|
CA
|
B:CYS153
|
4.6
|
0.0
|
1.0
|
H
|
B:GLY115
|
4.6
|
0.0
|
1.0
|
HB2
|
B:CYS153
|
4.7
|
0.0
|
1.0
|
O
|
B:ASN150
|
4.7
|
0.0
|
1.0
|
N
|
B:ASN150
|
4.7
|
0.0
|
1.0
|
CB
|
B:GLN151
|
4.7
|
0.0
|
1.0
|
HB3
|
B:HIS157
|
4.8
|
0.0
|
1.0
|
CB
|
B:MET160
|
4.8
|
0.0
|
1.0
|
H
|
B:TYR152
|
4.8
|
0.0
|
1.0
|
HB2
|
B:MET160
|
4.8
|
0.0
|
1.0
|
HA
|
B:CYS149
|
4.8
|
0.0
|
1.0
|
O
|
B:ILE113
|
4.8
|
0.0
|
1.0
|
CA
|
B:HIS114
|
4.9
|
0.0
|
1.0
|
HA
|
B:GLN151
|
4.9
|
0.0
|
1.0
|
HE2
|
B:HIS157
|
5.0
|
0.0
|
1.0
|
HB2
|
B:GLN151
|
5.0
|
0.0
|
1.0
|
|
Copper binding site 2 out
of 2 in 2fwl
Go back to
Copper Binding Sites List in 2fwl
Copper binding site 2 out
of 2 in the The Cytochrome C552/Cua Complex From Thermus Thermophilus
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of The Cytochrome C552/Cua Complex From Thermus Thermophilus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu169
b:0.0
occ:1.00
|
CU2
|
B:CUA169
|
0.0
|
0.0
|
1.0
|
ND1
|
B:HIS114
|
2.1
|
0.0
|
1.0
|
SG
|
B:CYS149
|
2.3
|
0.0
|
1.0
|
SG
|
B:CYS153
|
2.3
|
0.0
|
1.0
|
CU1
|
B:CUA169
|
2.4
|
0.0
|
1.0
|
SD
|
B:MET160
|
2.5
|
0.0
|
1.0
|
CE1
|
B:HIS114
|
2.9
|
0.0
|
1.0
|
HE1
|
B:HIS114
|
3.0
|
0.0
|
1.0
|
HA
|
B:HIS114
|
3.0
|
0.0
|
1.0
|
HB3
|
B:CYS153
|
3.1
|
0.0
|
1.0
|
CG
|
B:HIS114
|
3.2
|
0.0
|
1.0
|
CB
|
B:CYS153
|
3.3
|
0.0
|
1.0
|
HE3
|
B:MET160
|
3.4
|
0.0
|
1.0
|
CE
|
B:MET160
|
3.5
|
0.0
|
1.0
|
O
|
B:GLN151
|
3.5
|
0.0
|
1.0
|
HB3
|
B:HIS114
|
3.5
|
0.0
|
1.0
|
CB
|
B:CYS149
|
3.5
|
0.0
|
1.0
|
HB3
|
B:CYS149
|
3.6
|
0.0
|
1.0
|
HB2
|
B:CYS153
|
3.7
|
0.0
|
1.0
|
HE2
|
B:MET160
|
3.7
|
0.0
|
1.0
|
CB
|
B:HIS114
|
3.7
|
0.0
|
1.0
|
HB2
|
B:CYS149
|
3.8
|
0.0
|
1.0
|
O
|
B:ILE113
|
3.9
|
0.0
|
1.0
|
CA
|
B:HIS114
|
3.9
|
0.0
|
1.0
|
CG
|
B:MET160
|
3.9
|
0.0
|
1.0
|
HB3
|
B:MET160
|
4.0
|
0.0
|
1.0
|
H
|
B:GLY115
|
4.0
|
0.0
|
1.0
|
HG2
|
B:MET160
|
4.1
|
0.0
|
1.0
|
O
|
B:TYR152
|
4.1
|
0.0
|
1.0
|
NE2
|
B:HIS114
|
4.1
|
0.0
|
1.0
|
CD2
|
B:HIS114
|
4.3
|
0.0
|
1.0
|
HB2
|
B:MET160
|
4.3
|
0.0
|
1.0
|
CB
|
B:MET160
|
4.3
|
0.0
|
1.0
|
ND1
|
B:HIS157
|
4.4
|
0.0
|
1.0
|
HE1
|
B:MET160
|
4.4
|
0.0
|
1.0
|
HB2
|
B:HIS157
|
4.5
|
0.0
|
1.0
|
HA
|
B:HIS157
|
4.5
|
0.0
|
1.0
|
C
|
B:TYR152
|
4.6
|
0.0
|
1.0
|
CA
|
B:CYS153
|
4.7
|
0.0
|
1.0
|
C
|
B:GLN151
|
4.7
|
0.0
|
1.0
|
H
|
B:PHE88
|
4.7
|
0.0
|
1.0
|
C
|
B:ILE113
|
4.7
|
0.0
|
1.0
|
N
|
B:GLY115
|
4.7
|
0.0
|
1.0
|
HG3
|
B:MET160
|
4.8
|
0.0
|
1.0
|
HB3
|
B:GLN151
|
4.8
|
0.0
|
1.0
|
HB2
|
B:HIS114
|
4.8
|
0.0
|
1.0
|
O
|
B:CYS149
|
4.8
|
0.0
|
1.0
|
N
|
B:HIS114
|
4.8
|
0.0
|
1.0
|
N
|
B:CYS153
|
4.8
|
0.0
|
1.0
|
C
|
B:HIS114
|
4.9
|
0.0
|
1.0
|
HG23
|
B:VAL112
|
4.9
|
0.0
|
1.0
|
CA
|
B:CYS149
|
4.9
|
0.0
|
1.0
|
HA
|
B:PHE88
|
5.0
|
0.0
|
1.0
|
HE2
|
B:HIS114
|
5.0
|
0.0
|
1.0
|
OH
|
B:TYR90
|
5.0
|
0.0
|
1.0
|
|
Reference:
L.Muresanu,
P.Pristovsek,
F.Loehr,
O.Maneg,
M.D.Mukrasch,
H.Rueterjans,
B.Ludwig,
C.Luecke.
The Electron Transfer Complex Between Cytochrome C552 and the Cua Domain of the Thermus Thermophilus BA3 Oxidase - A Combined uc(Nmr) and Computational Approach J.Biol.Chem. V. 281 14503 2006.
ISSN: ISSN 0021-9258
PubMed: 16554303
DOI: 10.1074/JBC.M601108200
Page generated: Tue Jul 30 23:34:39 2024
|