Structure of PDB 1gt7 Chain N

Receptor sequence

>1gt7N (length=274) Species: 562 (Escherichia coli)

MQNITQSWFVQGMIKATTDAWLKGWDERNGGNLTLRLDDADIAPYHDNFH
QQPRYIPLSQPMPLLANTPFIVTGSGKFFRNVQLDPAANLGIVKVDSDGA
GYHILWGLTNEAVPTSELPAHFLSHCERIKATNGKDRVIMHCHATNLIAL
TYVLENDTAVFTRQLWEGSTECLVVFPDGVGILPWMVPGTDEIGQATAQE
MQKHSLVLWPFHGVFGSGPTLDETFGLIDTAEKSAQVLVKVYSMGGMKQT
ISREELIALGKRFGVTPLASALAL

3D structure

• PDB: 1gt7 The Structure of L-Rhamnulose-1-Phosphate Aldolase (Class II) Solved by Low-Resolution Sir Phasing and 20-Fold Ncs Averaging
• Chain: N
• Resolution: 2.7 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	N	H141 H143 H212	H141 H143 H212
BS02	PGH	N	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

External links

• PDB: RCSB:1gt7, PDBe:1gt7, PDBj:1gt7
• PDBsum: 1gt7
• PubMed: 11976494
• UniProt: P32169|RHAD_ECOLI Rhamnulose-1-phosphate aldolase (Gene Name=rhaD)