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1NDR

CRYSTALLOGRAPHIC STRUCTURE OF A BLUE COPPER NITRITE REDUCTASE FROM ALCALIGENES XYLOSOXIDANS

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
DetailsMONOMER A TYPE 1 COPPER SITE.
ChainResidue
AHIS95
ACYS136
AHIS145
AMET150

site_idAC2
Number of Residues4
DetailsMONOMER A TYPE 2 COPPER SITE.
ChainResidue
AHIS100
AHIS135
AHIS306
AHOH503

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 501
ChainResidue
AHIS95
ACYS136
AHIS145
AMET150

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 502
ChainResidue
AHIS100
AHIS135
AHOH503
BHIS306

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 501
ChainResidue
BHIS95
BCYS136
BHIS145
BMET150

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 502
ChainResidue
BHIS100
BHIS135
BHOH503
CHIS306

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

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU C 502
ChainResidue
AHIS306
AHOH504
CHIS100
CHIS135

site_idBC1
Number of Residues4
DetailsMONOMER B TYPE 1 COPPER SITE.
ChainResidue
BCYS136
BHIS145
BMET150
BHIS95

site_idBC2
Number of Residues4
DetailsMONOMER B TYPE 2 COPPER SITE.
ChainResidue
BHIS100
BHIS135
BHIS306
BHOH503

site_idCC1
Number of Residues4
DetailsMONOMER C TYPE 1 COPPER SITE.
ChainResidue
CHIS95
CCYS136
CHIS145
CMET150

site_idCC2
Number of Residues4
DetailsMONOMER C TYPE 2 COPPER SITE.
ChainResidue
CHIS100
CHIS135
CHIS306
AHOH504

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: type 1 copper site
ChainResidueDetails
AHIS95
CCYS136
CHIS145
CMET150
ACYS136
AHIS145
AMET150
BHIS95
BCYS136
BHIS145
BMET150
CHIS95

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: type 2 copper site
ChainResidueDetails
AHIS100
AHIS135
AHIS306
BHIS100
BHIS135
BHIS306
CHIS100
CHIS135
CHIS306

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 2024-07-10

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