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1LGT

CRYSTAL STRUCTURE OF 2,3-DIHYDROXYBIPHENYL 1,2-DIOXYGENASE (DHBD) COMPLEXED WITH 2'-Cl DIHYDROXYBIPHENYL (DHB)

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
ABP3300
AHOH9111

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE2 A 501
ChainResidue
AHOH9199
AHOH9200
AHIS189
AHOH9196
AHOH9197
AHOH9198

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE BP3 A 300
ChainResidue
AHIS146
AVAL148
AMET175
APHE187
AHIS195
AHIS210
AHIS241
AASN243
ATYR250
AGLU260
AFE2500
AHOH9111
AHOH9112

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BP3 A 301
ChainResidue
APHE110
APRO152
APRO205
ALYS206
AHIS209
AGLY256
AGLU258

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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