Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1L9P

CRYSTAL STRUCTURE OF NITRITE SOAKED I257G VARIANT OF THE COPPER-CONTAINING NITRITE REDUCTASE FROM ALCALIGENES FAECALIES S-6

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
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 Residues4
DetailsBINDING SITE FOR RESIDUE CU A 502
ChainResidue
AHIS100
AHIS135
ANO21504
BHIS306

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 501
ChainResidue
BCYS136
BHIS145
BMET150
BHIS95

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU B 502
ChainResidue
BHIS100
BHIS135
BNO22504
CHIS255
CHIS306

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU C 501
ChainResidue
CHIS95
CCYS136
CHIS145
CMET150

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU C 502
ChainResidue
AHIS306
CHIS100
CHIS135
CNO23504

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO2 A 1504
ChainResidue
AASP98
AHIS100
AHIS135
ACU502
BHIS255
BHIS306
BHOH6002

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO2 B 2504
ChainResidue
BASP98
BHIS100
BHIS135
BCU502
CHIS255
CHIS306

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO2 C 3504
ChainResidue
AHIS255
AGLY257
AHIS306
CASP98
CHIS100
CHIS135
CCU502
CHOH5531

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

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

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon