Structure of PDB 2bum Chain B

Receptor sequence
>2bumB (length=238) Species: 62977 (Acinetobacter baylyi ADP1) [Search protein sequence]
IIWGAYAQRNTEDHPPAYAPGYKTSVLRSPKNALISIAETLSEVTAPHFS
ADKFGPKDNDLILNYAKDGLPIGERVIVHGYVRDQFGRPVKNALVEVWQA
NASGRYRHPNDQYIGAMDPNFGGCGRMLTDDNGYYVFRTIKPGPYPWRNR
INEWRPAHIHFSLIADGWAQRLISQFYFEGDTLIDSCPILKTIPSEQQRR
ALIALEDKSNFIEADSRCYRFDITLRGRRATYFENDLT
3D structure
PDB2bum Biophysical Analyses of Designed and Selected Mutants of Protocatechuate 3,4-Dioxygenase
ChainB
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y408 Y447 R457 H460 H462
Catalytic site (residue number reindexed from 1) Y106 Y145 R155 H158 H160
Enzyme Commision number 1.13.11.3: protocatechuate 3,4-dioxygenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FE B Y408 Y447 H460 H462 Y106 Y145 H158 H160
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005506 iron ion binding
GO:0005515 protein binding
GO:0008199 ferric iron binding
GO:0016702 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
GO:0018578 protocatechuate 3,4-dioxygenase activity
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0009056 catabolic process
GO:0019619 3,4-dihydroxybenzoate catabolic process
GO:0042952 beta-ketoadipate pathway

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Molecular Function
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Biological Process
External links
PDB RCSB:2bum, PDBe:2bum, PDBj:2bum
PDBsum2bum
PubMed15487948
UniProtP20372|PCXB_ACIAD Protocatechuate 3,4-dioxygenase beta chain (Gene Name=pcaH)

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