Structure of PDB 1ojr Chain A

Receptor sequence

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

MQNITQSWFVQGMIKATTDAWLKGWDERNGGNLTLRLDDADIAPYHDNFH
QQPRYIPLSQPMPLLANTPFIVTGSGKFFRNVQLDPAANLGIVKVDSDGA
GYHILWGLTNEAVPTSELPAHFLSHCERIKATNGKDRVIMHCHATNLIAL
TYVLENDTAVFTRQLWEGSTECLVVFPDGVGILPWMVPGTDAIGQATAQE
MQKHSLVLWPFHGVFGSGPTLDETFGLIDTAEKSAQVLVKVYSMGGMKQT
ISREELIALGKRFGVTPLASALAL

3D structure

• PDB: 1ojr Structure and Catalytic Mechanism of L-Rhamnulose-1-Phosphate Aldolase.
• Chain: A
• Resolution: 1.35 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	A	H141 H143 H212	H141 H143 H212
BS02	PO4	A	N29 N32 S75 G76 T115 S116	N29 N32 S75 G76 T115 S116
BS03	PO4	A	N32 E117 H141 H212	N32 E117 H141 H212
BS04	2HA	A	N29 G30 G31 N32 E117 H141 H143 H212	N29 G30 G31 N32 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:1ojr, PDBe:1ojr, PDBj:1ojr
• PDBsum: 1ojr
• PubMed: 12962479
• UniProt: P32169|RHAD_ECOLI Rhamnulose-1-phosphate aldolase (Gene Name=rhaD)