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1KNF

Crystal Structure of 2,3-dihydroxybiphenyl 1,2-dioxygenase Complexed with 3-methyl Catechol under Anaerobic Condition

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005506molecular_functioniron ion binding
A0006725biological_processcellular aromatic compound metabolic process
A0008198molecular_functionferrous iron binding
A0016491molecular_functionoxidoreductase activity
A0018583molecular_functionbiphenyl-2,3-diol 1,2-dioxygenase activity
A0019439biological_processaromatic compound catabolic process
A0042178biological_processxenobiotic catabolic process
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FE2 A 500
ChainResidue
AHIS146
AHIS210
AGLU260
AMBD301
AHOH3001
AHOH3012
AHOH9001

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE FE2 A 501
ChainResidue
AHIS189

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE MBD A 301
ChainResidue
APHE187
AHIS195
AHIS210
AHIS241
AASN243
AASP244
ATYR250
AGLU260
AFE2500
AHOH3001
AHOH3012
AHOH9001
AHOH9002
AHIS146

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE TBU A 601
ChainResidue
ASER236
AARG289
ATBU600

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE TBU A 600
ChainResidue
ATYR250
APRO280
ATBU601

Functional Information from PROSITE/UniProt
site_idPS00082
Number of Residues22
DetailsEXTRADIOL_DIOXYGENAS Extradiol ring-cleavage dioxygenases signature. GrHtndhmvsFYasTPsGvevE
ChainResidueDetails
AGLY239-GLU260

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING:
ChainResidueDetails
APHE147
APHE211
ATYR261

217705

PDB entries from 2024-03-27

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