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1J9R

Crystal structure of nitrite soaked reduced D98N AFNIR

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0006807biological_processnitrogen compound metabolic process
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
B0006807biological_processnitrogen compound metabolic process
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
C0006807biological_processnitrogen compound metabolic process
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 Residues5
DetailsBINDING SITE FOR RESIDUE CU A 600
ChainResidue
AHIS95
ACYS136
APRO138
AHIS145
ACU601

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU A 601
ChainResidue
ACU600
AHIS95
ACYS136
AHIS145
AMET150

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 602
ChainResidue
AHIS100
AHIS135
ANO2604
BHIS306

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO2 A 604
ChainResidue
AASN98
AHIS100
AHIS135
ACU602
BHIS255
BILE257
BHIS306

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 700
ChainResidue
BCYS136
BPRO138
BHIS145
BCU701

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU B 701
ChainResidue
BHIS95
BCYS136
BHIS145
BMET150
BCU700

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 702
ChainResidue
BHIS100
BHIS135
BNO2704
CHIS306

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO2 B 704
ChainResidue
BASN98
BHIS100
BHIS135
BCU702
CHIS255
CILE257
CHIS306

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU C 800
ChainResidue
CCYS136
CPRO138
CHIS145
CCU801

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU C 801
ChainResidue
CHIS95
CCYS136
CHIS145
CMET150
CCU800

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU C 802
ChainResidue
AHIS306
CHIS100
CHIS135
CNO2804

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO2 C 804
ChainResidue
AILE257
AHIS306
CASN98
CHIS100
CHIS135
CCU802

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: type 1 copper site => ECO:0000269|PubMed:8172899
ChainResidueDetails
CHIS95
AHIS95
BHIS95

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: type 2 copper site
ChainResidueDetails
CHIS100
CHIS135
AHIS100
AHIS135
BHIS100
BHIS135

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: type 1 copper site
ChainResidueDetails
ACYS136
AHIS145
AMET150
BCYS136
BHIS145
BMET150
CCYS136
CHIS145
CMET150

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: type 2 copper site => ECO:0000269|PubMed:8172899
ChainResidueDetails
AHIS306
BHIS306
CHIS306

218500

PDB entries from 2024-04-17

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