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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
A0019333biological_processdenitrification pathway
A0042597cellular_componentperiplasmic space
A0050421molecular_functionnitrite reductase (NO-forming) activity
B0005507molecular_functioncopper ion binding
B0019333biological_processdenitrification pathway
B0042597cellular_componentperiplasmic space
B0050421molecular_functionnitrite reductase (NO-forming) activity
C0005507molecular_functioncopper ion binding
C0019333biological_processdenitrification pathway
C0042597cellular_componentperiplasmic space
C0050421molecular_functionnitrite reductase (NO-forming) activity
D0005507molecular_functioncopper ion binding
D0009055molecular_functionelectron transfer activity
D0042597cellular_componentperiplasmic space
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 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

site_idSWS_FT_FI5
Number of Residues88
DetailsDomain: {"description":"Plastocyanin-like"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"2909547","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nid
ChainResidueDetails
AASP98
AHIS255

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nid
ChainResidueDetails
BASP98
BHIS255

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nid
ChainResidueDetails
CASP98
CHIS255

251174

PDB entries from 2026-03-25

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