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1ET5

CRYSTAL STRUCTURE OF NITRITE REDUCTASE ASP98ASN MUTANT FROM ALCALIGENES FAECALIS S-6

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
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
AHOH503

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 504
ChainResidue
AHOH524
AHOH524
AHOH533
AHOH533
AHOH533
AHOH524

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 505
ChainResidue
AASP251
AASP251
AASP251

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBinding site: {"description":"type 1 copper site","evidences":[{"source":"PubMed","id":"8172899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"description":"type 2 copper site"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"description":"type 1 copper site"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
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
AASN98
AHIS255

246031

PDB entries from 2025-12-10

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