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2BUU

Crystal Structure Of Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1 Mutant R457S in complex with 4-Nitrocatechol

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 Residues4
DetailsBINDING SITE FOR RESIDUE FE B1541
ChainResidue
BTYR408
BHIS460
BHIS462
B4NC1542

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 4NC B1542
ChainResidue
BHIS460
BHIS462
BFE1541
BHOH2140
BHOH2142
APRO15
ATYR16
BTYR408
BTYR447
BTRP449

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

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
BSER457

222036

PDB entries from 2024-07-03

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