Structure of PDB 2ptx Chain A

Receptor sequence
>2ptxA (length=431) Species: 5691 (Trypanosoma brucei) [Search protein sequence]
SHMTIQKVHGREVLDSRGNPTVEVEVTTEKGVFRSAVPSGASTGVYEACE
LRDGDKKRYVGKGCLQAVKNVNEVIGPALIGRDELKQEELDTLMLRLDGT
PNKGKLGANAILGCSMAISKAAAAAKGVPLYRYLASLAGTKELRLPVPCF
NVINGGKHAGNALPFQEFMIAPVKATSFSEALRMGSEVYHSLRGIIKKKY
GQDAVNVGDEGGFAPPIKDINEPLPILMEAIEEAGHRGKFAICMDCAASE
TYDEKKQQYNLTFKSPEPTWVTAEQLRETYCKWAHDYPIVSIEDPYDQDD
FAGFAGITEALKGKTQIVGDDLTVTNTERIKMAIEKKACNSLLLKINQIG
TISEAIASSKLCMENGWSVMVSHRSGETEDTYIADLVVALGSGQIKTGAP
CRGERTAKLNQLLRIEEELGAHAKFGFPGWS
3D structure
PDB2ptx Structural flexibility in Trypanosoma brucei enolase revealed by X-ray crystallography and molecular dynamics.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 D243 E291 D318 D245 E293 D320
BS02 SO4 A G38 A39 S40 H156 R372 S373 G40 A41 S42 H158 R374 S375
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2ptx, PDBe:2ptx, PDBj:2ptx
PDBsum2ptx
PubMed17822439
UniProtQ38BV6

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