Structure of PDB 4b5v Chain B

Receptor sequence

>4b5vB (length=251) Species: 481805 (Escherichia coli ATCC 8739)

MENSFKAALKAGRPQIGLWLGLSSSYSAELLAGAGFDWLLIDGEHAPNNV
QTVLTQLQAIAPYPSQPVVRPSWNDPVQIKQLLDVGTQTLLVPMVQNADE
AREAVRATRYPPAGIRGVGSALARASRWNRIPDYLQKANDQMCVLVQIET
REAMKNLPQILDVEGVDGVFIGPADLSADMGYAGNPQHPEVQAAIEQAIV
QIRESGKAPGILIANEQLAKRYLELGALFVAVGVDTTLLARAAEALAARF
G

3D structure

• PDB: 4b5v Crystal Structure of Reaction Intermediates in Pyruvate Class II Aldolase: Substrate Cleavage, Enolate Stabilization and Substrate Specificity
• Chain: B
• Resolution: 2.041 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H45 R70 D84 E149 D175
• Catalytic site (residue number reindexed from 1): H45 R70 D84 E149 D175
• Enzyme Commision number: 4.1.2.52: 4-hydroxy-2-oxoheptanedioate aldolase.

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	PYR	B	F170 G172 P173 A174 D175 L212	F170 G172 P173 A174 D175 L212
BS02	E8U	B	R70 G172 P173 A174 L212	R70 G172 P173 A174 L212
BS03	MG	B	E149 D175	E149 D175

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0016829 lyase activity
• GO:0016832 aldehyde-lyase activity
• GO:0043863 4-hydroxy-2-ketopimelate aldolase activity
• GO:0046872 metal ion binding
• GO:0061677 2-dehydro-3-deoxy-D-gluconate aldolase activity

Biological Process

• GO:0009056 catabolic process
• GO:0010124 phenylacetate catabolic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:4b5v, PDBe:4b5v, PDBj:4b5v
• PDBsum: 4b5v
• PubMed: 22908224
• UniProt: B1IS70|HPCH_ECOLC 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (Gene Name=hpcH)