Structure of PDB 13pk Chain D

Receptor sequence
>13pkD (length=415) Species: 5691 (Trypanosoma brucei) [Search protein sequence]
EKKSINECDLKGKKVLIRVDFNVPVKNGKITNDYRIRSALPTLKKVLTEG
GSCVLMSHLGRPKGIPMAQAGKIRSTGGVPGFQQKATLKPVAKRLSELLL
RPVTFAPDCLNAADVVSKMSPGDVVLLENVRFYKEEGSKKAKDREAMAKI
LASYGDVYISDAFGTAHRDSATMTGIPKILGNGAAGYLMEKEISYFAKVL
GNPPRPLVAIVGGAKVSDKIQLLDNMLQRIDYLLIGGAMAYTFLKAQGYS
IGKSKCEESKLEFARSLLKKAEDRKVQVILPIDHVCHTEFKAVDSPLITE
DQNIPEGHMALDIGPKTIEKYVQTIGKCKSAIWNGPMGVFEMVPYSKGTF
AIAKAMGRGTHEHGLMSIIGGGDSASAAELSGEAKRMSHVSTGGGASLEL
LEGKTLPGVTVLDDK
3D structure
PDB13pk Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation.
ChainD
Resolution2.5 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 K219 G376 G399
Catalytic site (residue number reindexed from 1) R35 K215 G372 G395
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 ADP D G217 A218 Y245 P340 G342 V343 E345 G375 D377 S378 G213 A214 Y241 P336 G338 V339 E341 G371 D373 S374
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
GO:0020015 glycosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:13pk, PDBe:13pk, PDBj:13pk
PDBsum13pk
PubMed9000079
UniProtP07378|PGKC_TRYBB Phosphoglycerate kinase, glycosomal

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