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1L9O

CRYSTAL STRUCTURE OF NITRITE SOAKED I257A VARIANT OF THE COPPER-CONTAINING 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
AHIS145
AMET150

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CU A 502
ChainResidue
BNO2504
AHIS100
AHIS135
AHOH5294
BHIS255
BHIS306

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO2 B 504
ChainResidue
AHIS135
ACU502
AHOH5294
BHIS255
BALA257
BVAL304
BHIS306
BLEU308

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 501
ChainResidue
BHIS95
BCYS136
BHIS145
BMET150

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CU B 502
ChainResidue
BHIS100
BHIS135
CHIS255
CHIS306
CNO2604
CHOH5292

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO2 C 604
ChainResidue
BHIS135
BCU502
CHIS255
CALA257
CHIS306
CHOH5292
CHOH5612

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU C 501
ChainResidue
CHIS95
CCYS136
CHIS145
CMET150

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CU C 502
ChainResidue
AHIS255
AHIS306
ANO2704
AHOH5295
CHIS100
CHIS135

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO2 A 704
ChainResidue
AHIS255
AALA257
AHIS306
AHOH5295
CHIS135
CCU502

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

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PDB entries from 2026-02-18

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