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3HKP

Crystal structure determination of Catechol 1,2-Dioxygenase from Rhodococcus opacus 1CP in complex with protocatechuate

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
ADHB282

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE DHB A 282
ChainResidue
ATYR106
ATYR162
ATYR196
AARG217
AHIS220
AHIS222
AFE281
AHOH333
ALEU77
AASP80
AVAL81
AILE102
APRO105

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 6PL A 283
ChainResidue
AALA25
ATHR26
ATHR29
AILE37
ALEU45
ALEU45
AILE49
AGLU58
AVAL61
APHE62
ATRP65
AGLN206
APHE207

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

220760

PDB entries from 2024-06-05

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