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1KW3

Crystal structure of 2,3-dihydroxybiphenyal dioxygenase (BphC) at 1.45 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
B0003824molecular_functioncatalytic activity
B0005506molecular_functioniron ion binding
B0006725biological_processcellular aromatic compound metabolic process
B0008198molecular_functionferrous iron binding
B0016491molecular_functionoxidoreductase activity
B0018583molecular_functionbiphenyl-2,3-diol 1,2-dioxygenase activity
B0019439biological_processaromatic compound catabolic process
B0042178biological_processxenobiotic catabolic process
B0046872molecular_functionmetal ion binding
B0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE2 B 301
ChainResidue
BHIS145
BHIS209
BTYR249
BGLU260
BHOH564
BHOH800

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPD B 401
ChainResidue
BVAL133
BSER134
BHOH660
BHOH672
BPRO126
BPHE127
BPRO132

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MPD B 501
ChainResidue
BASP228
BLYS286

Functional Information from PROSITE/UniProt
site_idPS00082
Number of Residues21
DetailsEXTRADIOL_DIOXYGENAS Extradiol ring-cleavage dioxygenases signature. GrHtndqtlsFYadTPsPmi.E
ChainResidueDetails
BGLY238-GLU258

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING:
ChainResidueDetails
BPHE146
BPHE210
BPHE261

218500

PDB entries from 2024-04-17

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