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1KMY

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005506molecular_functioniron ion binding
A0006725biological_processobsolete cellular aromatic compound metabolic process
A0008198molecular_functionferrous iron binding
A0016491molecular_functionoxidoreductase activity
A0018583molecular_functionbiphenyl-2,3-diol 1,2-dioxygenase activity
A0019439biological_processobsolete aromatic compound catabolic process
A0042178biological_processxenobiotic catabolic process
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A 500
ChainResidue
AHIS146
AHIS210
AGLU260
ABPY300
AHOH9003

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE BPY A 300
ChainResidue
AHIS210
AHIS241
AASN243
AASP244
ATYR250
AGLU260
AFE2500
ATBU601
AHOH9002
AHOH9003
AHIS146
AMET175
APHE187
AHIS195

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE TBU A 601
ChainResidue
ASER236
AHIS285
AARG289
ABPY300

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

218853

PDB entries from 2024-04-24

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