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Copper in PDB 6gsq: Oxidised Copper Nitrite Reductase From Achromobacter Cycloclastes Determined By Serial Femtosecond Rotation Crystallography

Enzymatic activity of Oxidised Copper Nitrite Reductase From Achromobacter Cycloclastes Determined By Serial Femtosecond Rotation Crystallography

All present enzymatic activity of Oxidised Copper Nitrite Reductase From Achromobacter Cycloclastes Determined By Serial Femtosecond Rotation Crystallography:
1.7.2.1;

Protein crystallography data

The structure of Oxidised Copper Nitrite Reductase From Achromobacter Cycloclastes Determined By Serial Femtosecond Rotation Crystallography, PDB code: 6gsq was solved by T.P.Halsted, K.Yamashita, C.C.Gopalasingam, R.T.Shenoy, K.Hirata, H.Ago, G.Ueno, R.R.Eady, S.V.Antonyuk, M.Yamamoto, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 54.88 / 1.50
Space group P 21 3
Cell size a, b, c (Å), α, β, γ (°) 94.950, 94.950, 94.950, 90.00, 90.00, 90.00
R / Rfree (%) 14.4 / 17.7

Copper Binding Sites:

The binding sites of Copper atom in the Oxidised Copper Nitrite Reductase From Achromobacter Cycloclastes Determined By Serial Femtosecond Rotation Crystallography (pdb code 6gsq). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Oxidised Copper Nitrite Reductase From Achromobacter Cycloclastes Determined By Serial Femtosecond Rotation Crystallography, PDB code: 6gsq:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 6gsq

Go back to Copper Binding Sites List in 6gsq
Copper binding site 1 out of 2 in the Oxidised Copper Nitrite Reductase From Achromobacter Cycloclastes Determined By Serial Femtosecond Rotation Crystallography


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Oxidised Copper Nitrite Reductase From Achromobacter Cycloclastes Determined By Serial Femtosecond Rotation Crystallography within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:16.8
occ:1.00
ND1 A:HIS145 2.0 15.3 1.0
ND1 A:HIS95 2.0 15.4 1.0
SG A:CYS136 2.2 15.2 1.0
SD A:MET150 2.5 15.5 1.0
CE1 A:HIS145 2.9 16.4 1.0
CE1 A:HIS95 3.0 17.2 1.0
CG A:HIS95 3.0 15.6 1.0
CG A:HIS145 3.1 15.4 1.0
CB A:CYS136 3.2 15.2 1.0
CB A:HIS95 3.3 15.9 1.0
CE A:MET150 3.3 15.8 1.0
CB A:HIS145 3.5 15.3 1.0
CA A:HIS95 3.8 15.5 1.0
CG A:MET150 3.9 14.2 1.0
NE2 A:HIS145 4.1 16.0 1.0
CD2 A:HIS95 4.1 15.7 1.0
NE2 A:HIS95 4.1 16.4 1.0
CD2 A:HIS145 4.1 16.9 1.0
O A:LEU94 4.2 17.9 1.0
CB A:MET150 4.3 14.8 1.0
SD A:MET62 4.3 17.4 1.0
CG A:PRO138 4.3 17.0 1.0
CA A:CYS136 4.6 14.3 1.0
CA A:HIS145 4.7 15.1 1.0
N A:ASN96 4.7 16.1 1.0
CD A:PRO138 4.8 15.2 1.0
N A:HIS95 4.8 16.2 1.0
C A:HIS95 4.8 15.6 1.0
CB A:MET62 4.9 15.6 1.0
C A:LEU94 4.9 19.5 1.0

Copper binding site 2 out of 2 in 6gsq

Go back to Copper Binding Sites List in 6gsq
Copper binding site 2 out of 2 in the Oxidised Copper Nitrite Reductase From Achromobacter Cycloclastes Determined By Serial Femtosecond Rotation Crystallography


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Oxidised Copper Nitrite Reductase From Achromobacter Cycloclastes Determined By Serial Femtosecond Rotation Crystallography within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:16.2
occ:0.90
NE2 A:HIS100 2.0 14.1 1.0
NE2 A:HIS135 2.1 15.7 1.0
OD2 A:ASP98 2.5 15.7 0.5
CE1 A:HIS100 3.0 14.4 1.0
CD2 A:HIS100 3.0 13.3 1.0
CE1 A:HIS135 3.1 16.9 1.0
CD2 A:HIS135 3.1 16.1 1.0
OD2 A:ASP98 3.6 17.5 0.5
CG A:ASP98 3.7 19.6 0.5
ND1 A:HIS100 4.1 12.6 1.0
CG A:ASP98 4.1 17.5 0.5
O A:HOH702 4.1 21.1 1.0
CG A:HIS100 4.1 12.8 1.0
ND1 A:HIS135 4.2 15.7 1.0
CG A:HIS135 4.3 13.9 1.0
OD1 A:ASP98 4.3 16.1 0.5
OD1 A:ASP98 4.4 17.2 0.5
CB A:ASP98 4.6 17.8 0.5
O A:HOH778 4.6 17.0 1.0
CB A:ASP98 4.9 17.4 0.5

Reference:

T.P.Halsted, K.Yamashita, C.C.Gopalasingam, R.T.Shenoy, K.Hirata, H.Ago, G.Ueno, M.P.Blakeley, R.R.Eady, S.V.Antonyuk, M.Yamamoto, S.S.Hasnain. Catalytically Important Damage-Free Structures of A Copper Nitrite Reductase Obtained By Femtosecond X-Ray Laser and Room-Temperature Neutron Crystallography. Iucrj V. 6 761 2019.
ISSN: ESSN 2052-2525
PubMed: 31316819
DOI: 10.1107/S2052252519008285
Page generated: Sun Dec 13 11:22:40 2020

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