Atomistry » Copper » PDB 1rju-1tl4 » 1rzp
Atomistry »
  Copper »
    PDB 1rju-1tl4 »
      1rzp »

Copper in PDB 1rzp: Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase From Achromobacter Cycloclastes at PH6.2

Enzymatic activity of Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase From Achromobacter Cycloclastes at PH6.2

All present enzymatic activity of Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase From Achromobacter Cycloclastes at PH6.2:
1.7.2.1;

Protein crystallography data

The structure of Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase From Achromobacter Cycloclastes at PH6.2, PDB code: 1rzp was solved by H.T.Li, C.Wang, T.Chang, W.C.Chang, M.Y.Liu, J.Le Gall, L.L.Gui, J.P.Zhang, X.M.An, W.R.Chang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 98.880, 117.690, 123.030, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / 19.1

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase From Achromobacter Cycloclastes at PH6.2 (pdb code 1rzp). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase From Achromobacter Cycloclastes at PH6.2, PDB code: 1rzp:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in 1rzp

Go back to Copper Binding Sites List in 1rzp
Copper binding site 1 out of 6 in the Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase From Achromobacter Cycloclastes at PH6.2


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase From Achromobacter Cycloclastes at PH6.2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:19.8
occ:1.00
 ND1 A:HIS145 2.1 16.9 1.0
ND1 A:HIS95 2.2 18.2 1.0
SG A:CYS136 2.3 20.7 1.0
SD A:MET150 2.4 18.1 1.0
CE1 A:HIS145 2.9 17.7 1.0
CE1 A:HIS95 3.0 16.8 1.0
CB A:CYS136 3.1 18.7 1.0
CE A:MET150 3.1 15.8 1.0
CG A:HIS145 3.2 18.2 1.0
CG A:HIS95 3.2 18.2 1.0
CB A:HIS145 3.6 15.4 1.0
CB A:HIS95 3.6 18.4 1.0
CG A:MET150 3.8 15.8 1.0
CA A:HIS95 4.0 18.6 1.0
NE2 A:HIS145 4.1 17.6 1.0
CG A:PRO138 4.2 19.3 1.0
NE2 A:HIS95 4.2 16.8 1.0
CD2 A:HIS145 4.3 19.0 1.0
CD2 A:HIS95 4.3 15.9 1.0
CB A:MET150 4.3 14.2 1.0
O A:LEU94 4.4 19.0 1.0
SD A:MET62 4.5 18.5 1.0
CA A:CYS136 4.6 17.1 1.0
CD A:PRO138 4.6 18.0 1.0
N A:ASN96 4.8 19.0 1.0
CB A:MET62 4.8 17.6 1.0
CA A:HIS145 4.8 14.7 1.0

Copper binding site 2 out of 6 in 1rzp

Go back to Copper Binding Sites List in 1rzp
Copper binding site 2 out of 6 in the Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase From Achromobacter Cycloclastes at PH6.2


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase From Achromobacter Cycloclastes at PH6.2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:15.0
occ:1.00
 O A:HOH3003 1.9 25.0 1.0
NE2 A:HIS100 2.0 13.8 1.0
NE2 A:HIS135 2.1 11.8 1.0
NE2 B:HIS306 2.2 12.0 1.0
CE1 A:HIS100 2.9 11.7 1.0
CE1 B:HIS306 3.0 13.0 1.0
CE1 A:HIS135 3.1 13.6 1.0
CD2 A:HIS135 3.1 12.1 1.0
CD2 A:HIS100 3.1 13.2 1.0
CD2 B:HIS306 3.2 12.2 1.0
OD2 A:ASP98 3.6 23.7 1.0
NE2 B:HIS255 3.9 19.0 1.0
ND1 A:HIS100 4.1 12.4 1.0
ND1 A:HIS135 4.2 12.4 1.0
CG A:ASP98 4.2 21.8 1.0
ND1 B:HIS306 4.2 10.1 1.0
CG A:HIS100 4.2 12.4 1.0
CG A:HIS135 4.2 11.9 1.0
CD2 B:HIS255 4.3 19.4 1.0
CG B:HIS306 4.3 12.3 1.0
CE1 B:HIS255 4.4 16.9 1.0
OD1 A:ASP98 4.5 19.6 1.0
O B:HOH2038 4.9 18.3 1.0
CG B:HIS255 4.9 16.2 1.0
CD2 B:LEU308 5.0 15.0 1.0
ND1 B:HIS255 5.0 18.8 1.0

Copper binding site 3 out of 6 in 1rzp

Go back to Copper Binding Sites List in 1rzp
Copper binding site 3 out of 6 in the Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase From Achromobacter Cycloclastes at PH6.2


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase From Achromobacter Cycloclastes at PH6.2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu501

b:21.0
occ:1.00
 ND1 B:HIS145 2.2 19.5 1.0
ND1 B:HIS95 2.2 17.1 1.0
SG B:CYS136 2.3 22.8 1.0
SD B:MET150 2.4 18.5 1.0
CE1 B:HIS145 3.0 20.9 1.0
CE1 B:HIS95 3.0 18.6 1.0
CB B:CYS136 3.1 19.3 1.0
CG B:HIS95 3.2 18.5 1.0
CE B:MET150 3.2 15.3 1.0
CG B:HIS145 3.2 19.8 1.0
CB B:HIS95 3.6 19.0 1.0
CB B:HIS145 3.7 16.9 1.0
CG B:MET150 3.7 16.6 1.0
CA B:HIS95 4.0 21.1 1.0
NE2 B:HIS145 4.2 18.6 1.0
NE2 B:HIS95 4.2 17.3 1.0
CG B:PRO138 4.3 22.6 1.0
CD2 B:HIS95 4.3 18.1 1.0
CD2 B:HIS145 4.3 20.0 1.0
CB B:MET150 4.3 14.9 1.0
O B:LEU94 4.3 21.0 1.0
SD B:MET62 4.5 20.0 1.0
CA B:CYS136 4.6 17.9 1.0
CB B:MET62 4.8 18.5 1.0
N B:ASN96 4.8 21.7 1.0
CA B:HIS145 4.8 16.8 1.0
CD B:PRO138 4.9 20.4 1.0
C B:HIS95 5.0 21.7 1.0

Copper binding site 4 out of 6 in 1rzp

Go back to Copper Binding Sites List in 1rzp
Copper binding site 4 out of 6 in the Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase From Achromobacter Cycloclastes at PH6.2


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase From Achromobacter Cycloclastes at PH6.2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu502

b:16.8
occ:1.00
 O B:HOH2003 1.9 23.0 1.0
NE2 B:HIS100 2.0 14.8 1.0
NE2 B:HIS135 2.1 12.7 1.0
NE2 C:HIS306 2.2 15.8 1.0
CE1 B:HIS100 2.9 12.3 1.0
CD2 B:HIS135 3.1 12.6 1.0
CE1 C:HIS306 3.1 15.9 1.0
CD2 B:HIS100 3.1 15.1 1.0
CE1 B:HIS135 3.1 13.1 1.0
CD2 C:HIS306 3.3 15.8 1.0
OD2 B:ASP98 3.7 25.5 1.0
NE2 C:HIS255 3.8 20.3 1.0
ND1 B:HIS100 4.1 11.8 1.0
CG B:HIS100 4.2 14.4 1.0
CG B:ASP98 4.2 24.8 1.0
ND1 B:HIS135 4.2 12.7 1.0
CG B:HIS135 4.2 11.9 1.0
ND1 C:HIS306 4.2 14.1 1.0
CD2 C:HIS255 4.2 20.3 1.0
CE1 C:HIS255 4.3 19.1 1.0
CG C:HIS306 4.4 15.4 1.0
OD1 B:ASP98 4.4 21.1 1.0
O C:HOH3108 4.8 21.6 1.0
CG C:HIS255 4.9 17.9 1.0
ND1 C:HIS255 4.9 19.0 1.0

Copper binding site 5 out of 6 in 1rzp

Go back to Copper Binding Sites List in 1rzp
Copper binding site 5 out of 6 in the Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase From Achromobacter Cycloclastes at PH6.2


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase From Achromobacter Cycloclastes at PH6.2 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu501

b:19.9
occ:1.00
 ND1 C:HIS95 2.1 14.2 1.0
ND1 C:HIS145 2.2 19.4 1.0
SG C:CYS136 2.3 16.4 1.0
SD C:MET150 2.5 16.9 1.0
CE1 C:HIS95 3.0 12.9 1.0
CE1 C:HIS145 3.0 18.6 1.0
CB C:CYS136 3.1 15.8 1.0
CE C:MET150 3.2 12.5 1.0
CG C:HIS95 3.2 12.9 1.0
CG C:HIS145 3.2 18.7 1.0
CB C:HIS95 3.6 13.4 1.0
CB C:HIS145 3.6 16.8 1.0
CG C:MET150 3.8 15.3 1.0
CA C:HIS95 3.9 13.3 1.0
O C:LEU94 4.2 14.3 1.0
NE2 C:HIS145 4.2 18.6 1.0
NE2 C:HIS95 4.2 14.1 1.0
CG C:PRO138 4.3 19.9 1.0
CD2 C:HIS145 4.3 18.9 1.0
CD2 C:HIS95 4.3 12.1 1.0
CB C:MET150 4.3 13.8 1.0
SD C:MET62 4.5 17.7 1.0
CA C:CYS136 4.5 14.3 1.0
CD C:PRO138 4.6 15.9 1.0
N C:ASN96 4.8 13.9 1.0
CA C:HIS145 4.8 15.2 1.0
CB C:MET62 4.8 13.3 1.0
N C:HIS95 4.9 14.6 1.0
C C:HIS95 4.9 14.1 1.0
C C:LEU94 5.0 15.4 1.0

Copper binding site 6 out of 6 in 1rzp

Go back to Copper Binding Sites List in 1rzp
Copper binding site 6 out of 6 in the Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase From Achromobacter Cycloclastes at PH6.2


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase From Achromobacter Cycloclastes at PH6.2 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu502

b:13.9
occ:1.00
 O C:HOH3002 1.9 23.8 1.0
NE2 C:HIS100 2.0 10.2 1.0
NE2 C:HIS135 2.1 12.7 1.0
NE2 A:HIS306 2.2 14.0 1.0
CE1 C:HIS100 2.9 10.3 1.0
CE1 A:HIS306 3.0 12.1 1.0
CD2 C:HIS135 3.0 12.0 1.0
CE1 C:HIS135 3.1 12.3 1.0
CD2 C:HIS100 3.1 9.7 1.0
CD2 A:HIS306 3.2 11.8 1.0
OD2 C:ASP98 3.7 20.8 1.0
NE2 A:HIS255 3.9 19.3 1.0
ND1 C:HIS100 4.0 9.2 1.0
ND1 A:HIS306 4.2 11.6 1.0
CG C:HIS100 4.2 10.3 1.0
ND1 C:HIS135 4.2 12.2 1.0
CG C:HIS135 4.2 12.6 1.0
CG C:ASP98 4.2 18.5 1.0
CD2 A:HIS255 4.3 18.9 1.0
CG A:HIS306 4.3 11.4 1.0
CE1 A:HIS255 4.4 18.2 1.0
OD1 C:ASP98 4.5 15.2 1.0
O C:HOH3014 4.9 15.2 1.0
CG A:HIS255 4.9 16.3 1.0
ND1 A:HIS255 5.0 17.2 1.0

Reference:

H.T.Li, C.Wang, T.Chang, W.C.Chang, M.Y.Liu, J.Le Gall, L.L.Gui, J.P.Zhang, X.M.An, W.R.Chang. pH-Profile Crystal Structure Studies of C-Terminal Despentapeptide Nitrite Reductase From Achromobacter Cycloclastes Biochem.Biophys.Res.Commun. V. 316 107 2004.
ISSN: ISSN 0006-291X
PubMed: 15003518
DOI: 10.1016/J.BBRC.2004.01.177
Page generated: Tue Jul 30 22:43:07 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy