Structure of PDB 3srk Chain B

Receptor sequence
>3srkB (length=405) Species: 5665 (Leishmania mexicana) [Search protein sequence]
MSQLAHNLTLSIFDPVANYRAARIICTIGPSTQSVEALKGLIQSGMSVAR
MNFSHGSHEYHQTTINNVRQAAAELGVNIAIALDTKGPEVNLPGCDVDLP
AVSAKDRVDLQFGVEQGVDMIFASFIRSAEQVGDVRKALGPKGRDIMIIC
KIENHQGVQNIDSIIEESDGIMVARGDLGVEIPAEKVVVAQKILISKCNV
AGKPVICATQMLESMTYNPRPTRAEVSDVANAVFNGADCVMLSGETAKGK
YPNEVVQYMARICLEAQSALNEYVFFNSIKKLQHIPMSADEAVCSSAVNS
VYETKAKAMVVLSNTGRSARLVAKYRPNCPIVCVTTRLQTCRQLNITQGV
ESVFFDADKLGHDEGKEHRVAAGVEFAKSKGYVQTGDYCVVIHAYANQTR
ILLVE
3D structure
PDB3srk A new class of suicide inhibitor blocks nucleotide binding to pyruvate kinase
ChainB
Resolution2.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R49 K238 T296
Catalytic site (residue number reindexed from 1) R50 K151 T209
Enzyme Commision number 2.7.1.40: pyruvate 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 LSA B H54 G55 Y59 K335 H55 G56 Y60 K248
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0004743 pyruvate kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0030955 potassium ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006096 glycolytic process
GO:0016310 phosphorylation
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3srk, PDBe:3srk, PDBj:3srk
PDBsum3srk
PubMed
UniProtQ27686|KPYK_LEIME Pyruvate kinase (Gene Name=PYK)

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