Structure of PDB 2uyv Chain A Binding Site BS01

Receptor Information

>2uyv Chain A (length=274) Species: 562 (Escherichia coli)

MQNITYSWFVQGMIKATTDAWLKGWDERNGGNLTLRLDDADIAPYHDNFH
QQPRYIPLSQPMPLLANTPFIVTGSGKFFRNVQLDPAANLGIVKVDSDGA
GYHILWGLTNEAVPTSELPAHFLSHCERIKATNGKDRVIMHCHATNLIAL
TYVLENDTAVFTRQLWEGSTECLVVFPDGVGILPWMVPGTDAIGQATAQE
MQKHSLVLWPFHGVFGSGPTLDETFGLIDTAEKSAQVLVKVYSMGGMKQT
ISREELIALGKRFGVTPLASALAL

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 2uyv Chain A Residue 1276

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2uyv Designed Protein-Protein Association.
• Resolution: 2.2 Å
• Binding residue (original residue number in PDB): H141 H143 H212
• Binding residue (residue number reindexed from 1): H141 H143 H212
• Annotation score: 1

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.

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:2uyv, PDBe:2uyv, PDBj:2uyv
• PDBsum: 2uyv
• PubMed: 18187656
• UniProt: P32169|RHAD_ECOLI Rhamnulose-1-phosphate aldolase (Gene Name=rhaD)