Copper in PDB 6zav: No-Bound Copper Nitrite Reductase From Bradyrhizobium Sp. Ors 375 (Two-Domain) at 1.19 A Resolution (Unrestrained, Full Matrix Refinement By Shelx)

Enzymatic activity of No-Bound Copper Nitrite Reductase From Bradyrhizobium Sp. Ors 375 (Two-Domain) at 1.19 A Resolution (Unrestrained, Full Matrix Refinement By Shelx)

All present enzymatic activity of No-Bound Copper Nitrite Reductase From Bradyrhizobium Sp. Ors 375 (Two-Domain) at 1.19 A Resolution (Unrestrained, Full Matrix Refinement By Shelx):
1.7.2.1;

Protein crystallography data

The structure of No-Bound Copper Nitrite Reductase From Bradyrhizobium Sp. Ors 375 (Two-Domain) at 1.19 A Resolution (Unrestrained, Full Matrix Refinement By Shelx), PDB code: 6zav was solved by S.L.Rose, S.V.Antonyuk, D.Sasaki, K.Yamashita, K.Hirata, G.Ueno, H.Ago, R.R.Eady, T.Tosha, M.Yamamoto, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.19
Space group P 21 3
Cell size a, b, c (Å), α, β, γ (°) 107.467, 107.467, 107.467, 90, 90, 90
R / Rfree (%) n/a / n/a

Copper Binding Sites:

The binding sites of Copper atom in the No-Bound Copper Nitrite Reductase From Bradyrhizobium Sp. Ors 375 (Two-Domain) at 1.19 A Resolution (Unrestrained, Full Matrix Refinement By Shelx) (pdb code 6zav). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the No-Bound Copper Nitrite Reductase From Bradyrhizobium Sp. Ors 375 (Two-Domain) at 1.19 A Resolution (Unrestrained, Full Matrix Refinement By Shelx), PDB code: 6zav:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 6zav

Go back to Copper Binding Sites List in 6zav
Copper binding site 1 out of 2 in the No-Bound Copper Nitrite Reductase From Bradyrhizobium Sp. Ors 375 (Two-Domain) at 1.19 A Resolution (Unrestrained, Full Matrix Refinement By Shelx)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of No-Bound Copper Nitrite Reductase From Bradyrhizobium Sp. Ors 375 (Two-Domain) at 1.19 A Resolution (Unrestrained, Full Matrix Refinement By Shelx) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:14.0
occ:1.00
 ND1 A:HIS89 2.1 11.9 1.0
ND1 A:HIS140 2.1 12.5 1.0
SG A:CYS130 2.2 12.6 1.0
SD A:MET145 2.5 13.1 1.0
CE1 A:HIS140 3.0 12.6 1.0
CE1 A:HIS89 3.0 12.2 1.0
CG A:HIS89 3.1 11.9 1.0
CG A:HIS140 3.2 12.5 1.0
CB A:CYS130 3.2 12.7 1.0
CE A:MET145 3.3 14.2 1.0
CB A:HIS89 3.5 11.6 1.0
CB A:HIS140 3.5 11.8 1.0
CA A:HIS89 3.8 12.0 1.0
CG A:MET145 3.9 13.7 1.0
NE2 A:HIS140 4.2 13.4 1.0
NE2 A:HIS89 4.2 11.6 1.0
O A:PRO88 4.2 13.6 1.0
CD2 A:HIS140 4.2 13.7 1.0
CG A:PRO132 4.2 14.2 0.6
CD2 A:HIS89 4.2 12.2 1.0
CG A:PRO132 4.3 15.8 0.4
CB A:MET145 4.5 11.9 1.0
SD A:MET56 4.6 14.2 0.3
CD A:PRO132 4.6 11.9 0.6
CA A:CYS130 4.7 11.2 1.0
N A:ASN90 4.7 12.0 1.0
CA A:HIS140 4.7 11.3 1.0
C A:HIS89 4.8 12.2 1.0
N A:HIS89 4.9 12.5 1.0
CD A:PRO132 4.9 13.5 0.4
C A:PRO88 4.9 12.6 1.0
CE A:MET56 5.0 13.4 0.7

Copper binding site 2 out of 2 in 6zav

Go back to Copper Binding Sites List in 6zav
Copper binding site 2 out of 2 in the No-Bound Copper Nitrite Reductase From Bradyrhizobium Sp. Ors 375 (Two-Domain) at 1.19 A Resolution (Unrestrained, Full Matrix Refinement By Shelx)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of No-Bound Copper Nitrite Reductase From Bradyrhizobium Sp. Ors 375 (Two-Domain) at 1.19 A Resolution (Unrestrained, Full Matrix Refinement By Shelx) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:13.9
occ:1.00
 NE2 A:HIS129 2.0 12.0 1.0
NE2 A:HIS94 2.0 10.7 1.0
O A:NO503 2.1 23.8 0.7
N A:NO503 2.2 29.0 0.7
CD2 A:HIS129 2.9 12.1 1.0
CE1 A:HIS94 2.9 10.6 1.0
CE1 A:HIS129 3.0 12.3 1.0
CD2 A:HIS94 3.1 10.7 1.0
OD2 A:ASP92 3.7 20.6 0.8
ND1 A:HIS94 4.1 10.2 1.0
CG A:HIS129 4.1 10.7 1.0
ND1 A:HIS129 4.1 11.6 1.0
CG A:HIS94 4.2 9.7 1.0
O A:HOH629 4.2 32.6 0.5
CG A:ASP92 4.4 15.2 0.8
OD1 A:ASP92 4.6 15.6 0.8

Reference:

S.L.Rose, S.V.Antonyuk, D.Sasaki, K.Yamashita, K.Hirata, G.Ueno, H.Ago, R.R.Eady, T.Tosha, M.Yamamoto, S.S.Hasnain. An Unprecedented Insight Into the Catalytic Mechanism of Copper Nitrite Reductase From Atomic-Resolution and Damage-Free Structures Sci Adv V. 7 2021.
ISSN: ESSN 2375-2548
DOI: 10.1126/SCIADV.ABD8523
Page generated: Sun Jan 24 15:06:59 2021

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy