Structure of PDB 2wvk Chain A Binding Site BS01

Receptor Information

>2wvk Chain A (length=391) Species: 262724 (Thermus thermophilus HB27)

MRLEIPNHTERFGVVRLHEVQRILELDSGRVRDESPAVGLRRLDDADLRD
VLEQTAIVVPTRNERLKLLEGVLSGIPHEALILVASNSSPDRFQMERDLL
EEFAHLTERPALIFHQKDPALAEALRAGGYPHPIGEDGLVRSGKAEGMIL
ALVFAALSGRRYVGFIDADNYFPGAVWEYVRAYAAGFLMAKTPFAMVRIL
WRYKPKLTEDEGVVFRRYGRVSERNNRALNQLIGGVSGFETDVVKTANAG
EHAMSLGLALRLPLASGYAVEPQELVSLLELYGGVFPLEDEEVLQHGVEI
FQIETRNPHLHENKGDEHIRDMLLACLATVYHSKLATEEVRQSVLEELQA
AGALAPGEEPPPPVLYPPLSSLDLQAVRKALRGHFSRFRVP

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: 2wvk Chain A Residue 1393

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2wvk Structural Analysis of Thermus Thermophilus Hb27 Mannosyl-3-Phosphoglycerate Synthase Provides Evidence for a Second Catalytic Metal Ion and New Insight Into the Retaining Mechanism of Glycosyltransferases.
• Resolution: 2.97 Å
• Binding residue (original residue number in PDB): H8 E19
• Binding residue (residue number reindexed from 1): H8 E19
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 2.4.1.-

Gene Ontology

Molecular Function

• GO:0016757 glycosyltransferase activity
• GO:0046872 metal ion binding
• GO:0050504 mannosyl-3-phosphoglycerate synthase activity

Biological Process

• GO:0051479 mannosylglycerate biosynthetic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:2wvk, PDBe:2wvk, PDBj:2wvk
• PDBsum: 2wvk
• PubMed: 20356840
• UniProt: Q72K30