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1NPN

Crystal structure of a copper reconstituted H145A mutant of nitrite reductase from Alcaligenes faecalis

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0016491molecular_functionoxidoreductase activity
A0019333biological_processdenitrification pathway
A0042128biological_processnitrate assimilation
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
A0050421molecular_functionnitrite reductase (NO-forming) activity
B0005507molecular_functioncopper ion binding
B0016491molecular_functionoxidoreductase activity
B0019333biological_processdenitrification pathway
B0042128biological_processnitrate assimilation
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
B0050421molecular_functionnitrite reductase (NO-forming) activity
C0005507molecular_functioncopper ion binding
C0016491molecular_functionoxidoreductase activity
C0019333biological_processdenitrification pathway
C0042128biological_processnitrate assimilation
C0042597cellular_componentperiplasmic space
C0046872molecular_functionmetal ion binding
C0050421molecular_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
AMET150
ACL498

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 502
ChainResidue
AHIS100
AHIS135
BHIS306
BHOH503

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 498
ChainResidue
AALA145
ACU501
AHIS95

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 501
ChainResidue
BHIS95
BCYS136
BMET150
BCL499

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 502
ChainResidue
BHIS100
BHIS135
CHIS306
CHOH504

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 499
ChainResidue
BMET62
BHIS95
BMET141
BALA145
BCU501

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU C 501
ChainResidue
CHIS95
CCYS136
CMET150
CCL500

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU C 502
ChainResidue
AHIS306
AHOH505
CHIS100
CHIS135

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL C 500
ChainResidue
CMET62
CHIS95
CALA145
CCU501

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBinding site: {"description":"type 1 copper site","evidences":[{"source":"PubMed","id":"8172899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"description":"type 2 copper site"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues9
DetailsBinding site: {"description":"type 1 copper site"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"description":"type 2 copper site","evidences":[{"source":"PubMed","id":"8172899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nid
ChainResidueDetails
APHE64
AGLY66

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nid
ChainResidueDetails
BPHE64
BGLY66

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nid
ChainResidueDetails
CPHE64
CGLY66

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nid
ChainResidueDetails
AASP98
AHIS255

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nid
ChainResidueDetails
BASP98
BHIS255

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nid
ChainResidueDetails
CASP98
CHIS255

239149

PDB entries from 2025-07-23

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