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

2DWT

Cu-containing nitrite reductase at pH 6.0 with bound nitrite

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 401
ChainResidue
AHIS126
ACYS167
AHIS177
AMET182

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 402
ChainResidue
AHIS131
AHIS166
AHIS338
ANO2501

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO2 A 501
ChainResidue
AHIS131
AHIS166
AHIS287
AILE289
AHIS338
ALEU340
ACU402
AASP129

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NO2 A 502
ChainResidue
AHIS60
AGLN62

Functional Information from PROSITE/UniProt
site_idPS00283
Number of Residues17
DetailsSOYBEAN_KUNITZ Soybean trypsin inhibitor (Kunitz) protease inhibitors family signature. LkDHEGKpVrYDtvYyI
ChainResidueDetails
ALEU194-ILE210

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: type 1 copper site => ECO:0000250
ChainResidueDetails
AHIS126
ACYS167
AHIS177
AMET182

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: type 2 copper site => ECO:0000250
ChainResidueDetails
AHIS131
AHIS166
AHIS338

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon