Structure of PDB 1gt7 Chain F

Receptor sequence
>1gt7F (length=274) Species: 562 (Escherichia coli) [Search protein sequence]
MQNITQSWFVQGMIKATTDAWLKGWDERNGGNLTLRLDDADIAPYHDNFH
QQPRYIPLSQPMPLLANTPFIVTGSGKFFRNVQLDPAANLGIVKVDSDGA
GYHILWGLTNEAVPTSELPAHFLSHCERIKATNGKDRVIMHCHATNLIAL
TYVLENDTAVFTRQLWEGSTECLVVFPDGVGILPWMVPGTDEIGQATAQE
MQKHSLVLWPFHGVFGSGPTLDETFGLIDTAEKSAQVLVKVYSMGGMKQT
ISREELIALGKRFGVTPLASALAL
3D structure
PDB1gt7 The Structure of L-Rhamnulose-1-Phosphate Aldolase (Class II) Solved by Low-Resolution Sir Phasing and 20-Fold Ncs Averaging
ChainF
Resolution2.7 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 F H141 H143 H212 H141 H143 H212
BS02 PGH F N29 G30 G31 N32 S75 G76 T115 S116 E117 H141 H143 H212 N29 G30 G31 N32 S75 G76 T115 S116 E117 H141 H143 H212
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:1gt7, PDBe:1gt7, PDBj:1gt7
PDBsum1gt7
PubMed11976494
UniProtP32169|RHAD_ECOLI Rhamnulose-1-phosphate aldolase (Gene Name=rhaD)

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