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1HAN

CRYSTAL STRUCTURE OF THE BIPHENYL-CLEAVING EXTRADIOL DIOXYGENASE FROM A PCB-DEGRADING PSEUDOMONAD

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 FE A 500
ChainResidue
AHOH3012
AHIS146
AHIS210
AGLU260
AHOH3001

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE FE A 501
ChainResidue
AHIS189

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE TBU A 600
ChainResidue
APHE202
AHIS209
ATYR250
APRO280

site_idFE1
Number of Residues5
DetailsACTIVE SITE: FE(II) BINDING SITE CONSISTING IN THE FIRST SHELL OF THREE PROTEIN RESIDUES AND TWO SOLVENT SPECIES, WHICH MAY BE HOH OR OH- BUT WERE REFINED AS HOH
ChainResidue
AHIS146
AHIS210
AGLU260
AHOH3001
AHOH3012

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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