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6GBY

Copper nitrite reductase from Achromobacter cycloclastes: non-polymorph separated dataset 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0006807biological_processobsolete nitrogen compound metabolic process
A0050421molecular_functionnitrite reductase (NO-forming) activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CU A 501
ChainResidue
AHIS95
ACYS136
AHIS145
AMET150

site_idAC2
Number of Residues4
Detailsbinding site for residue CU A 502
ChainResidue
AHIS100
AHIS135
AHIS306
ANO2503

site_idAC3
Number of Residues8
Detailsbinding site for residue NO2 A 503
ChainResidue
AHIS100
AHIS135
AHIS255
AILE257
AHIS306
ALEU308
ACU502
AASP98

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: type 1 copper site
ChainResidueDetails
AHIS95
ACYS136
AHIS145
AMET150

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: type 2 copper site
ChainResidueDetails
AHIS100
AHIS135
AHIS306

Catalytic Information from CSA
site_idMCSA1
Number of Residues11
DetailsM-CSA 4
ChainResidueDetails
AHIS95metal ligand
ATHR280electrostatic stabiliser, modifies pKa
AHIS306metal ligand
AASP98activator, hydrogen bond acceptor, proton acceptor, proton donor
AHIS100metal ligand
AHIS135metal ligand, single electron acceptor, single electron donor, single electron relay
ACYS136metal ligand, single electron acceptor, single electron donor, single electron relay
AHIS145metal ligand
AMET150metal ligand
AHIS255hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLU279electrostatic stabiliser, modifies pKa

218853

PDB entries from 2024-04-24

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