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5ZNH

Catechol 2,3-dioxygenase with 4-methyl catechol from Diaphorobacter sp DS2

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0008198molecular_functionferrous iron binding
A0009056biological_processcatabolic process
A0018577molecular_functioncatechol 2,3-dioxygenase activity
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue FE A 401
ChainResidue
AHIS150
AHIS220
AGLU271
AMCT402

site_idAC2
Number of Residues13
Detailsbinding site for residue MCT A 402
ChainResidue
AILE254
ATHR255
ATYR261
AGLU271
APHE273
AALA297
AILE298
AFE401
AHIS150
APHE198
AHIS206
AHIS220
AHIS252

site_idAC3
Number of Residues3
Detailsbinding site for residue PEG A 403
ChainResidue
AGLY162
AASN164
AASP168

site_idAC4
Number of Residues3
Detailsbinding site for residue EDO A 404
ChainResidue
ATHR97
ALEU98
AARG116

site_idAC5
Number of Residues5
Detailsbinding site for residue CA A 405
ChainResidue
AASP149
ATHR204
AHIS206
AASP207
AHOH506

Functional Information from PROSITE/UniProt
site_idPS00082
Number of Residues22
DetailsEXTRADIOL_DIOXYGENAS Extradiol ring-cleavage dioxygenases signature. TrHgitrgetIYffDPsGnrnE
ChainResidueDetails
ATHR250-GLU271

222926

PDB entries from 2024-07-24

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