Structure of PDB 1eo2 Chain B

Receptor sequence

>1eo2B (length=238) Species: 62977 (Acinetobacter baylyi ADP1)

IIWGAYAQRNTEDHPPAYAPGYKTSVLRSPKNALISIAETLSEVTAPHFS
ADKFGPKDNDLILNYAKDGLPIGERVIVHGYVRDQFGRPVKNALVEVWQA
NASGRYRHPNDQYIGAMDPNFGGCGRMLTDDNGYYVFRTIKPGPYPWRNR
INEWRPAHIHFSLIADGWAQRLISQFYFEGDTLIDSCPILKTIPSEQQRR
ALIALEDKSNFIEADSRCYRFDITLRGRRATYFENDLT

3D structure

• PDB: 1eo2 Structure of Acinetobacter strain ADP1 protocatechuate 3, 4-dioxygenase at 2.2 A resolution: implications for the mechanism of an intradiol dioxygenase.
• Chain: B
• Resolution: 2.25 Å

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

External links

• PDB: RCSB:1eo2, PDBe:1eo2, PDBj:1eo2
• PDBsum: 1eo2
• PubMed: 10891075
• UniProt: P20372|PCXB_ACIAD Protocatechuate 3,4-dioxygenase beta chain (Gene Name=pcaH)