Structure of PDB 2v29 Chain A

Receptor sequence
>2v29A (length=274) Species: 562 (Escherichia coli) [Search protein sequence]
MQNITQSWFVQGMIWATTDAWLKGWDERNGGNLTLRLDDADIAPYHDNFH
QQPRYIPLSQPMPLLANTPFIVTGSGKFFRNVQLDPAANLGIVKVDSDGA
GYHILWGLTNEAVPTSELPAHFLSHCERIKATNGKDRVIMHCHATNLIAL
TYVLENDTAVFTRQLWEGSTECLVVFPDGVGILPWMVPGTDEIGQATAQE
MQKHSLVLWPFHGVFGSGPTLDETFGLIDTAEKSAQVLVKVYSMGGMKQT
ISREELIALGKRFGVTPLASALAL
3D structure
PDB2v29 Antenna Domain Mobility and Enzymatic Reaction of L-Rhamnulose-1-Phosphate Aldolase.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 A H141 H143 H212 H141 H143 H212
BS02 ZN A H46 D47 H46 D47
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

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Cellular Component
External links
PDB RCSB:2v29, PDBe:2v29, PDBj:2v29
PDBsum2v29
PubMed18085797
UniProtP32169|RHAD_ECOLI Rhamnulose-1-phosphate aldolase (Gene Name=rhaD)

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