Structure of PDB 2pu1 Chain A Binding Site BS01

Receptor Information

>2pu1 Chain A (length=431) Species: 5691 (Trypanosoma brucei)

SHMTIQKVHGREVLDSRGNPTVEVEVTTEKGVFRSAVPSGASTGVYEACE
LRDGDKKRYVGKGCLQAVKNVNEVIGPALIGRDELKQEELDTLMLRLDGT
PNKGKLGANAILGCSMAISKAAAAAKGVPLYRYLASLAGTKELRLPVPCF
NVINGGKHAGNALPFQEFMIAPVKATSFSEALRMGSEVYHSLRGIIKKKY
GQDAVNVGDEGGFAPPIKDINEPLPILMEAIEEAGHRGKFAICMDCAASE
TYDEKKQQYNLTFKSPEPTWVTAEQLRETYCKWAHDYPIVSIEDPYDQDD
FAGFAGITEALKGKTQIVGDDLTVTNTERIKMAIEKKACNSLLLKINQIG
TISEAIASSKLCMENGWSVMVSHRSGETEDTYIADLVVALGSGQIKTGAP
CRGERTAKLNQLLRIEEELGAHAKFGFPGWS

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: 2pu1 Chain A Residue 500

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2pu1 Structural flexibility in Trypanosoma brucei enolase revealed by X-ray crystallography and molecular dynamics.
• Resolution: 1.8 Å
• Binding residue (original residue number in PDB): D243 E291 D318
• Binding residue (residue number reindexed from 1): D245 E293 D320
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): S40 H156 E165 E208 D243 E291 D318 K343 H371 K394
• Catalytic site (residue number reindexed from 1): S42 H158 E167 E210 D245 E293 D320 K345 H373 K396
• Enzyme Commision number: 4.2.1.11: phosphopyruvate hydratase.

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0004634 phosphopyruvate hydratase activity
• GO:0016829 lyase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006096 glycolytic process

Cellular Component

• GO:0000015 phosphopyruvate hydratase complex
• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0097014 ciliary plasm

External links

• PDB: RCSB:2pu1, PDBe:2pu1, PDBj:2pu1
• PDBsum: 2pu1
• PubMed: 17822439
• UniProt: Q9NDH8