Structure of PDB 2pu0 Chain A Binding Site BS03

Receptor Information
>2pu0 Chain A (length=431) Species: 5691 (Trypanosoma brucei) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SHMTIQKVHGREVLDSRGNPTVEVEVTTEKGVFRSAVPSGASTGVYEACE
LRDGDKKRYVGKGCLQAVKNVNEVIGPALIGRDELKQEELDTLMLRLDGT
PNKGKLGANAILGCSMAISKAAAAAKGVPLYRYLASLAGTKELRLPVPCF
NVINGGKHAGNALPFQEFMIAPVKATSFSEALRMGSEVYHSLRGIIKKKY
GQDAVNVGDEGGFAPPIKDINEPLPILMEAIEEAGHRGKFAICMDCAASE
TYDEKKQQYNLTFKSPEPTWVTAEQLRETYCKWAHDYPIVSIEDPYDQDD
FAGFAGITEALKGKTQIVGDDLTVTNTERIKMAIEKKACNSLLLKINQIG
TISEAIASSKLCMENGWSVMVSHRSGETEDTYIADLVVALGSGQIKTGAP
CRGERTAKLNQLLRIEEELGAHAKFGFPGWS
Ligand information
Ligand IDPAH
InChIInChI=1S/C2H6NO5P/c4-2(3-5)1-9(6,7)8/h5H,1H2,(H,3,4)(H2,6,7,8)
InChIKeyLDKRAXXVBWHMRH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(NO)CP(=O)(O)O
CACTVS 3.341ONC(=O)C[P](O)(O)=O
OpenEye OEToolkits 1.5.0C(C(=O)NO)P(=O)(O)O
FormulaC2 H6 N O5 P
NamePHOSPHONOACETOHYDROXAMIC ACID
ChEMBLCHEMBL328944
DrugBankDB03645
ZINCZINC000005828202
PDB chain2pu0 Chain A Residue 600 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2pu0 Structural flexibility in Trypanosoma brucei enolase revealed by X-ray crystallography and molecular dynamics.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		G38 A39 S40 H156 Q164 E165 D243 D318 K343 R372 S373 K394
Binding residue
(residue number reindexed from 1)		G40 A41 S42 H158 Q166 E167 D245 D320 K345 R374 S375 K396
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=7.82,Ki=15nM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2pu0, PDBe:2pu0, PDBj:2pu0
PDBsum2pu0
PubMed17822439
UniProtQ38BV6

[Back to BioLiP]