Structure of PDB 1ltk Chain C

Receptor sequence
>1ltkC (length=424) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
HSMHHHHHHLGNKLSISDLKDIKNKKVLVRVDFNVPIENGIIKDTNRITA
TLPTINHLKKEGASKIILISHCGRPDGLRNEKYTLKPVAETLKGLLGEEV
LFLNDCVGKEVEDKINAAKENSVILLENLRFHIEEEGKGVDANGNKVKAN
KEDVEKFQNDLTKLADVFINDAFGTAHRAHSSMVGVKLNVKASGFLMKKE
LEYFSKALENPQRPLLAILGGAKVSDKIQLIKNLLDKVDRMIIGGGMAYT
FKKVLNNMKIGTSLFDEAGSKIVGEIMEKAKAKNVQIFLPVDFKIADNFD
NNANTKFVTDEEGIPDNWMGLDAGPKSIENYKDVILTSKTVIWNGPQGVF
EMPNFAKGSIECLNLVVEVTKKGAITIVGGGDTASLVEQQNKKNEISHVS
TGGGASLELLEGKELPGVLALSNK
3D structure
PDB1ltk CRYSTAL STRUCTURE OF PHOSPHOGLYCERATE KINASE FROM PLASMODIUM FALCIPARUM
ChainC
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R39 K215 G373 G396
Catalytic site (residue number reindexed from 1) R47 K223 G381 G404
Enzyme Commision number 2.7.2.3: phosphoglycerate kinase.
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 AMP C G213 A214 K215 G237 G238 G340 V341 E343 D374 G221 A222 K223 G245 G246 G348 V349 E351 D382
Gene Ontology
Molecular Function
GO:0004618 phosphoglycerate kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0043531 ADP binding
Biological Process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0016310 phosphorylation
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ltk, PDBe:1ltk, PDBj:1ltk
PDBsum1ltk
PubMed
UniProtP27362|PGK_PLAF7 Phosphoglycerate kinase (Gene Name=PGK)

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