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2BUX

Crystal Structure of Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1 Mutant R133H

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0006725biological_processobsolete cellular aromatic compound metabolic process
A0008199molecular_functionferric iron binding
A0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A0018578molecular_functionprotocatechuate 3,4-dioxygenase activity
A0019439biological_processobsolete aromatic compound catabolic process
A0042952biological_processbeta-ketoadipate pathway
A0051213molecular_functiondioxygenase activity
B0003824molecular_functioncatalytic activity
B0005506molecular_functioniron ion binding
B0005515molecular_functionprotein binding
B0006725biological_processobsolete cellular aromatic compound metabolic process
B0008199molecular_functionferric iron binding
B0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
B0018578molecular_functionprotocatechuate 3,4-dioxygenase activity
B0019439biological_processobsolete aromatic compound catabolic process
B0019619biological_process3,4-dihydroxybenzoate catabolic process
B0042952biological_processbeta-ketoadipate pathway
B0046872molecular_functionmetal ion binding
B0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE B 1541
ChainResidue
BTYR408
BTYR447
BHIS460
BHIS462
BOH1542

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OH B 1542
ChainResidue
BFE1541
BHOH2154
APRO15
BTYR408
BTYR447
BHIS462

Functional Information from PROSITE/UniProt
site_idPS00083
Number of Residues29
DetailsINTRADIOL_DIOXYGENAS Intradiol ring-cleavage dioxygenases signature. LeGqVfdglGlpLrdvlIEIwqadtnGvY
ChainResidueDetails
ALEU51-TYR79
BVAL380-TYR408

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BTYR408
BTYR447
BHIS460
BHIS462

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 3pca
ChainResidueDetails
BTYR447
BARG457

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PDB entries from 2024-05-01

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