Atomistry » Copper » PDB 3f00-3ie9 » 3h4h
Atomistry »
  Copper »
    PDB 3f00-3ie9 »
      3h4h »

Copper in PDB 3h4h: MET94THR/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis

Enzymatic activity of MET94THR/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis

All present enzymatic activity of MET94THR/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis:
1.7.2.1;

Protein crystallography data

The structure of MET94THR/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis, PDB code: 3h4h was solved by I.S.Macpherson, I.S.Murphy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 61.301, 102.077, 146.336, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 22.6

Copper Binding Sites:

The binding sites of Copper atom in the MET94THR/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis (pdb code 3h4h). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the MET94THR/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis, PDB code: 3h4h:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in 3h4h

Go back to Copper Binding Sites List in 3h4h
Copper binding site 1 out of 6 in the MET94THR/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of MET94THR/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1501

b:14.2
occ:1.00
 ND1 A:HIS145 2.0 12.3 1.0
ND1 A:HIS95 2.1 13.2 1.0
SG A:CYS136 2.2 13.6 1.0
SD A:MET150 2.5 13.2 1.0
CE1 A:HIS145 2.8 13.4 1.0
CE1 A:HIS95 3.0 14.3 1.0
CG A:HIS145 3.1 12.4 1.0
CB A:CYS136 3.1 11.7 1.0
CG A:HIS95 3.1 12.1 1.0
CE A:MET150 3.3 14.3 1.0
CB A:HIS95 3.5 13.6 1.0
CB A:HIS145 3.5 12.7 1.0
CA A:HIS95 3.8 13.2 1.0
CG A:MET150 3.9 11.3 1.0
NE2 A:HIS145 4.0 13.9 1.0
CD2 A:HIS145 4.1 15.3 1.0
NE2 A:HIS95 4.2 12.4 1.0
CG A:PRO138 4.2 17.3 1.0
CD2 A:HIS95 4.2 13.1 1.0
O A:THR94 4.3 16.5 1.0
CB A:MET150 4.3 10.2 1.0
SD A:MET62 4.3 15.5 1.0
CD A:PRO138 4.6 14.4 1.0
CA A:CYS136 4.6 12.1 1.0
N A:ASN96 4.6 12.3 1.0
CA A:HIS145 4.7 12.1 1.0
CB A:MET62 4.8 14.1 1.0
C A:HIS95 4.8 13.1 1.0
N A:HIS95 4.9 13.9 1.0
C A:THR94 5.0 15.7 1.0

Copper binding site 2 out of 6 in 3h4h

Go back to Copper Binding Sites List in 3h4h
Copper binding site 2 out of 6 in the MET94THR/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of MET94THR/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1502

b:13.6
occ:1.00
 O A:HOH1337 1.9 25.6 1.0
NE2 A:HIS135 2.0 12.2 1.0
NE2 B:HIS306 2.0 13.1 1.0
NE2 A:HIS100 2.1 10.1 1.0
CD2 A:HIS135 3.0 13.1 1.0
CE1 A:HIS100 3.0 9.8 1.0
CE1 B:HIS306 3.0 9.6 1.0
CD2 B:HIS306 3.0 11.1 1.0
CE1 A:HIS135 3.1 13.1 1.0
CD2 A:HIS100 3.1 12.7 1.0
O B:HOH1347 3.4 68.6 1.0
OD1 A:ASP98 3.8 20.9 1.0
O A:HOH480 4.0 32.3 1.0
NE2 B:HIS255 4.1 13.9 1.0
CG A:HIS135 4.1 12.8 1.0
ND1 A:HIS100 4.1 12.4 1.0
ND1 B:HIS306 4.1 11.3 1.0
ND1 A:HIS135 4.1 11.7 1.0
CG B:HIS306 4.2 10.8 1.0
CG A:HIS100 4.2 10.9 1.0
CG A:ASP98 4.2 17.4 1.0
CE1 B:HIS255 4.4 14.8 1.0
CD2 B:HIS255 4.5 13.9 1.0
OD2 A:ASP98 4.5 15.1 1.0
O A:HOH511 4.6 53.5 1.0
O B:HOH532 4.8 16.9 1.0
ND1 B:HIS255 4.8 17.0 1.0
CG B:HIS255 4.9 13.1 1.0
CD1 B:LEU308 4.9 15.7 1.0

Copper binding site 3 out of 6 in 3h4h

Go back to Copper Binding Sites List in 3h4h
Copper binding site 3 out of 6 in the MET94THR/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of MET94THR/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu2501

b:18.2
occ:1.00
 ND1 B:HIS95 2.1 14.8 1.0
ND1 B:HIS145 2.1 19.1 1.0
SG B:CYS136 2.2 17.6 1.0
SD B:MET150 2.5 16.2 1.0
CE1 B:HIS145 3.0 21.4 1.0
CE1 B:HIS95 3.0 18.6 1.0
CG B:HIS95 3.1 17.3 1.0
CG B:HIS145 3.2 19.2 1.0
CB B:CYS136 3.2 16.2 1.0
CE B:MET150 3.4 17.5 1.0
CB B:HIS95 3.5 18.3 1.0
CB B:HIS145 3.6 18.8 1.0
CA B:HIS95 3.9 18.6 1.0
CG B:MET150 4.0 14.9 1.0
NE2 B:HIS145 4.1 18.8 1.0
NE2 B:HIS95 4.1 16.2 1.0
CG B:PRO138 4.2 21.4 1.0
O B:THR94 4.2 20.1 1.0
CD2 B:HIS145 4.2 19.2 1.0
CD2 B:HIS95 4.2 16.6 1.0
SD B:MET62 4.3 18.3 1.0
CB B:MET150 4.4 13.8 1.0
CA B:CYS136 4.6 16.2 1.0
CD B:PRO138 4.6 21.2 1.0
N B:ASN96 4.7 18.0 1.0
CA B:HIS145 4.8 18.1 1.0
CB B:MET62 4.8 16.6 1.0
C B:HIS95 4.8 18.7 1.0
N B:HIS95 4.9 19.4 1.0
C B:THR94 4.9 19.7 1.0

Copper binding site 4 out of 6 in 3h4h

Go back to Copper Binding Sites List in 3h4h
Copper binding site 4 out of 6 in the MET94THR/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of MET94THR/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu2502

b:17.9
occ:1.00
 O B:HOH1346 2.0 31.1 1.0
NE2 B:HIS135 2.0 15.1 1.0
NE2 B:HIS100 2.1 16.6 1.0
NE2 C:HIS306 2.1 14.3 1.0
CE1 B:HIS100 3.0 13.7 1.0
CD2 B:HIS135 3.0 14.6 1.0
CE1 B:HIS135 3.0 13.4 1.0
CD2 C:HIS306 3.1 16.3 1.0
CE1 C:HIS306 3.1 15.2 1.0
CD2 B:HIS100 3.1 16.9 1.0
OD1 B:ASP98 3.5 25.8 1.0
O B:HOH423 3.8 42.3 1.0
NE2 C:HIS255 4.0 19.9 1.0
ND1 B:HIS100 4.1 13.9 1.0
ND1 B:HIS135 4.1 14.6 1.0
CG B:HIS135 4.2 12.9 1.0
CG B:ASP98 4.2 21.1 1.0
ND1 C:HIS306 4.2 16.3 1.0
CG C:HIS306 4.2 13.6 1.0
CG B:HIS100 4.2 14.4 1.0
CD2 C:HIS255 4.3 20.8 1.0
CE1 C:HIS255 4.4 19.1 1.0
OD2 B:ASP98 4.6 19.0 1.0
CG C:HIS255 4.8 17.9 1.0
ND1 C:HIS255 4.8 19.3 1.0
O B:HOH544 4.8 20.3 1.0
CD1 C:LEU308 5.0 16.6 1.0

Copper binding site 5 out of 6 in 3h4h

Go back to Copper Binding Sites List in 3h4h
Copper binding site 5 out of 6 in the MET94THR/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of MET94THR/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu3501

b:23.7
occ:1.00
 ND1 C:HIS145 2.0 21.9 1.0
ND1 C:HIS95 2.1 23.1 1.0
SG C:CYS136 2.2 21.8 1.0
SD C:MET150 2.5 20.1 1.0
CE1 C:HIS145 2.9 24.1 1.0
CE1 C:HIS95 3.0 23.4 1.0
CG C:HIS145 3.1 22.8 1.0
CB C:CYS136 3.1 22.3 1.0
CE C:MET150 3.2 20.3 1.0
CG C:HIS95 3.2 23.8 1.0
CB C:HIS145 3.5 22.0 1.0
CB C:HIS95 3.6 24.4 1.0
CG C:MET150 3.8 20.5 1.0
CA C:HIS95 3.8 24.5 1.0
NE2 C:HIS145 4.0 25.9 1.0
CD2 C:HIS145 4.1 23.9 1.0
NE2 C:HIS95 4.2 22.4 1.0
O C:THR94 4.2 27.0 1.0
CG C:PRO138 4.2 26.9 1.0
CD2 C:HIS95 4.3 24.9 1.0
CB C:MET150 4.3 20.7 1.0
SD C:MET62 4.5 23.1 1.0
CA C:CYS136 4.5 22.4 1.0
N C:ASN96 4.6 24.4 1.0
CD C:PRO138 4.6 25.8 1.0
CA C:HIS145 4.8 22.2 1.0
C C:HIS95 4.8 24.5 1.0
CB C:MET62 4.8 21.6 1.0
N C:HIS95 4.9 25.5 1.0
C C:THR94 4.9 26.3 1.0

Copper binding site 6 out of 6 in 3h4h

Go back to Copper Binding Sites List in 3h4h
Copper binding site 6 out of 6 in the MET94THR/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of MET94THR/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu3502

b:20.5
occ:1.00
 O C:HOH1339 2.0 32.9 1.0
NE2 C:HIS100 2.0 19.2 1.0
NE2 C:HIS135 2.1 19.8 1.0
NE2 A:HIS306 2.1 16.0 1.0
CE1 C:HIS100 2.9 17.2 1.0
CD2 C:HIS135 3.0 18.6 1.0
CE1 A:HIS306 3.0 18.4 1.0
CD2 C:HIS100 3.1 18.3 1.0
CD2 A:HIS306 3.1 18.5 1.0
CE1 C:HIS135 3.1 17.5 1.0
OD1 C:ASP98 3.6 29.7 1.0
ND1 C:HIS100 4.1 19.2 1.0
O C:HOH667 4.1 42.2 1.0
ND1 A:HIS306 4.2 17.8 1.0
CG C:HIS135 4.2 19.2 1.0
CG C:HIS100 4.2 20.2 1.0
NE2 A:HIS255 4.2 21.3 1.0
ND1 C:HIS135 4.2 19.0 1.0
CG A:HIS306 4.3 15.5 1.0
CG C:ASP98 4.3 24.6 1.0
CE1 A:HIS255 4.4 24.6 1.0
CD2 A:HIS255 4.5 22.4 1.0
OD2 C:ASP98 4.7 23.9 1.0
ND1 A:HIS255 4.8 21.8 1.0
O A:HOH379 4.9 25.4 1.0
CG A:HIS255 4.9 19.2 1.0
CD1 A:LEU308 4.9 21.6 1.0
CG1 A:ILE257 5.0 22.3 1.0

Reference:

I.S.Macpherson, F.I.Rosell, M.Scofield, A.G.Mauk, M.E.Murphy. Directed Evolution of Copper Nitrite Reductase to A Chromogenic Reductant. Protein Eng.Des.Sel. V. 23 137 2010.
ISSN: ISSN 1741-0126
PubMed: 20083495
DOI: 10.1093/PROTEIN/GZP084
Page generated: Wed Jul 31 01:00:35 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy