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3N9T

Cryatal structure of Hydroxyquinol 1,2-dioxygenase from Pseudomonas putida DLL-E4

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005506molecular_functioniron ion binding
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
A0018576molecular_functioncatechol 1,2-dioxygenase activity
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HGX A 300
ChainResidue
APRO24
AGLN140
AARG142
AALA208
AASN25
APHE28
AGLU52
ATRP53
AILE57
APHE59
APHE75
ALEU78

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE FLC A 293
ChainResidue
ALEU77
AASP80
APRO107
APHE108
ATYR160
ATYR194
AILE196
APRO197
AARG215
AHIS218
AHIS220
AVAL248
AFE292
AHOH313

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 292
ChainResidue
ATYR160
ATYR194
AHIS218
AHIS220
AFLC293
AHOH313

Functional Information from PROSITE/UniProt
site_idPS00083
Number of Residues29
DetailsINTRADIOL_DIOXYGENAS Intradiol ring-cleavage dioxygenases signature. VyGrVldvqGrpVvgavLDVwqtadnGmY
ChainResidueDetails
AVAL132-TYR160

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PDB entries from 2024-07-31

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