Structure of PDB 2v29 Chain B

Receptor sequence

>2v29B (length=274) Species: 562 (Escherichia coli)

MQNITQSWFVQGMIWATTDAWLKGWDERNGGNLTLRLDDADIAPYHDNFH
QQPRYIPLSQPMPLLANTPFIVTGSGKFFRNVQLDPAANLGIVKVDSDGA
GYHILWGLTNEAVPTSELPAHFLSHCERIKATNGKDRVIMHCHATNLIAL
TYVLENDTAVFTRQLWEGSTECLVVFPDGVGILPWMVPGTDEIGQATAQE
MQKHSLVLWPFHGVFGSGPTLDETFGLIDTAEKSAQVLVKVYSMGGMKQT
ISREELIALGKRFGVTPLASALAL

3D structure

• PDB: 2v29 Antenna Domain Mobility and Enzymatic Reaction of L-Rhamnulose-1-Phosphate Aldolase.
• Chain: B
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E117 H141 H143 E171 H212
• Catalytic site (residue number reindexed from 1): E117 H141 H143 E171 H212
• Enzyme Commision number: 4.1.2.19: rhamnulose-1-phosphate 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	ZN	B	D47 H50	D47 H50
BS02	ZN	B	H141 H143 H212	H141 H143 H212
BS03	ZN	B	E200 H204	E200 H204

Gene Ontology

Molecular Function

• GO:0008994 rhamnulose-1-phosphate aldolase activity
• GO:0016829 lyase activity
• GO:0016830 carbon-carbon lyase activity
• GO:0016832 aldehyde-lyase activity
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding

Biological Process

• GO:0005996 monosaccharide metabolic process
• GO:0019299 rhamnose metabolic process
• GO:0019301 rhamnose catabolic process
• GO:0019323 pentose catabolic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:2v29, PDBe:2v29, PDBj:2v29
• PDBsum: 2v29
• PubMed: 18085797
• UniProt: P32169|RHAD_ECOLI Rhamnulose-1-phosphate aldolase (Gene Name=rhaD)