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2P80

Solution structure of the complex between nitrite reductase and pseudoazurin from A. faecalis

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0006807biological_processobsolete nitrogen 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_processobsolete nitrogen 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_processobsolete nitrogen 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
D0005507molecular_functioncopper ion binding
D0009055molecular_functionelectron transfer activity
D0042597cellular_componentperiplasmic space
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 345
ChainResidue
AHIS95
ACYS136
AHIS145
AMET150

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU A 346
ChainResidue
AHIS100
AHIS135
BHIS306

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 345
ChainResidue
BHIS145
BMET150
BHIS95
BCYS136

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU B 346
ChainResidue
BHIS100
BHIS135
CHIS306

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU C 345
ChainResidue
CHIS95
CCYS136
CHIS145
CMET150

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU C 346
ChainResidue
AHIS306
CHIS100
CHIS135

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU D 124
ChainResidue
DHIS40
DCYS78
DHIS81
DMET86

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GD A 347
ChainResidue
ALYS231

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GD C 347
ChainResidue
CLYS231

Functional Information from PROSITE/UniProt
site_idPS00196
Number of Residues15
DetailsCOPPER_BLUE Type-1 copper (blue) proteins signature. Ga.YlVKCt.P.HyamgM
ChainResidueDetails
DGLY72-MET86

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:2909547
ChainResidueDetails
DHIS40
DCYS78
DHIS81
DMET86

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

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

218853

PDB entries from 2024-04-24

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