Structure of PDB 4whq Chain B

Receptor sequence

>4whqB (length=238) Species: 303 (Pseudomonas putida)

PAQDNSRFVIRDRNWHPKALTPDYKTSIARSPRQALVSIPQSISETTGPN
FSHLGFGAHDHDLLLNFNNGGLPIGERIIVAGRVVDQYGKPVPNTLVEMW
QANAGGRYRHKNDRYLAPLDPNFGGVGRCLTDSDGYYSFRTIKPGPYPWR
NGPNDWRPAHIHFGISGPSIATKLITQLYFEGDPLIPMCPIVKSIANPEA
VQQLIAKLDMNNANPMDCLAYRFDIVLRGQRKTHFENC

3D structure

• PDB: 4whq Crystal structures of alkylperoxo and anhydride intermediates in an intradiol ring-cleaving dioxygenase.
• Chain: B
• Resolution: 1.78 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y408 Y447 R457 H460 H462
• Catalytic site (residue number reindexed from 1): Y108 Y147 R157 H160 H162
• 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	Y108 Y147 H160 H162
BS02	3N8	B	K493 I495 A496 V501	K193 I195 A196 V201
BS03	3N8	B	R383 D524	R83 D224
BS04	3N8	B	R409 H410 K411	R109 H110 K111
BS05	3N9	B	Y408 Y447 W449 R457 H460 H462 I491	Y108 Y147 W149 R157 H160 H162 I191

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0005506 iron ion 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:4whq, PDBe:4whq, PDBj:4whq
• PDBsum: 4whq
• PubMed: 25548185
• UniProt: P00437|PCXB_PSEPU Protocatechuate 3,4-dioxygenase beta chain (Gene Name=pcaH)