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3HJS

Crystal structure of catechol 1,2-dioxygenase from Rhodococcus opacus 1CP in complex with 4-methylcatechol

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005506molecular_functioniron ion binding
A0006725biological_processobsolete cellular aromatic compound metabolic process
A0008199molecular_functionferric iron binding
A0009712biological_processcatechol-containing compound metabolic process
A0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A0018575molecular_functionchlorocatechol 1,2-dioxygenase activity
A0018576molecular_functioncatechol 1,2-dioxygenase activity
A0019439biological_processobsolete aromatic compound catabolic process
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE A 281
ChainResidue
ATYR162
AHIS220
AHIS222
AMCT283

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 282
ChainResidue
AASP142
AHOH326
AHOH386

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MCT A 283
ChainResidue
AGLY104
APRO105
ATYR106
ATYR162
ATYR196
AARG217
AHIS220
AHIS222
AFE281
AASP80
AVAL81

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 6PL A 284
ChainResidue
ATHR29
ALEU45
AGLU58
AVAL61
APHE62
APHE62
ATRP65
ALEU79
AGLN206

Functional Information from PROSITE/UniProt
site_idPS00083
Number of Residues29
DetailsINTRADIOL_DIOXYGENAS Intradiol ring-cleavage dioxygenases signature. FsGqVtdldGngLagakVELwhadndGyY
ChainResidueDetails
APHE134-TYR162

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ATYR162
ATYR196
AHIS220
AHIS222

219140

PDB entries from 2024-05-01

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