Structure of PDB 4b5s Chain A

Receptor sequence
>4b5sA (length=251) Species: 481805 (Escherichia coli ATCC 8739) [Search protein sequence]
MENSFKAALKAGRPQIGLWLGLSSSYSAELLAGAGFDWLLIDGEHAPNNV
QTVLTQLQAIAPYPSQPVVRPSWNDPVQIKQLLDVGTQTLLVPMVQNADE
AREAVRATRYPPAGIRGVGSALARASRWNRIPDYLQKANDQMCVLVQIET
REAMKNLPQILDVEGVDGVFIGPADLSADMGYAGNPQHPEVQAAIEQAIV
QIRESGKAPGILIANEQLAKRYLELGALFVAVGVDTTLLARAAEALAARF
G
3D structure
PDB4b5s Crystal Structure of Reaction Intermediates in Pyruvate Class II Aldolase: Substrate Cleavage, Enolate Stabilization and Substrate Specificity
ChainA
Resolution1.68 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 CO A E149 D175 E149 D175
BS02 PYR A E149 F170 G172 P173 A174 D175 E149 F170 G172 P173 A174 D175 PDBbind-CN: -logKd/Ki=3.49,Kd=0.32mM
BS03 MG A 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

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External links
PDB RCSB:4b5s, PDBe:4b5s, PDBj:4b5s
PDBsum4b5s
PubMed22908224
UniProtB1IS70|HPCH_ECOLC 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (Gene Name=hpcH)

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