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2BUW

Crystal Structure of Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1 Mutant R457S in Complex with 4-Hydroxybenzoate

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
A0016491molecular_functionoxidoreductase activity
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
B0016491molecular_functionoxidoreductase activity
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 600
ChainResidue
BTYR408
BTYR447
BHIS460
BHIS462
BPHB999

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PHB B 999
ChainResidue
BTYR408
BTYR447
BTRP449
BHIS460
BHIS462
BFE600
BHOH2100
BHOH2152
BHOH2153
AGLY14
APRO15
AARG133
BTYR324

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

218853

PDB entries from 2024-04-24

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