Structure of PDB 3hqo Chain K

Receptor sequence
>3hqoK (length=491) Species: 5665 (Leishmania mexicana) [Search protein sequence]
SQLAHNLTLSIFDPVANYRAARIICTIGPSTQSVEALKGLIQSGMSVARM
NFSHGSHEYHQTTINNVRQAAAELGVNIAIALDTKGPEIRTGQFVGGDAV
MERGATCYVTTDPAFADKGTKDKFYIDYQNLSKVVRPGNYIYIDDGILIL
QVQSHEDEQTLECTVTNSHTISDRRGVNLPGCDVDLPAVSAKDRVDLQFG
VEQGVDMIFASFIRSAEQVGDVRKALGPKGRDIMIICKIENHQGVQNIDS
IIEESDGIMVARGDLGVEIPAEKVVVAQKILISKCNVAGKPVICATQMLE
SMTYNPRPTRAEVSDVANAVFNGADCVMLSGETAKGKYPNEVVQYMARIC
LEAQSALNEYVFFNSIKKLQHIPMSADEAVCSSAVNSVYETKAKAMVVLS
NTGRSARLVAKYRPNCPIVCVTTRLQTCRQLNITQGVESVFFDADKLGHD
EGKEHRVAAGVEFAKSKGYVQTGDYCVVIHYANQTRILLVE
3D structure
PDB3hqo The allosteric mechanism of pryuvate kinase from Leishmania mexicana: a rock and lock model
ChainK
Resolution3.4 Å
3D
structure
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Enzymatic activity
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 MG K E240 D264 E240 D264
BS02 OXL K K238 E240 A261 G263 D264 T296 K238 E240 A261 G263 D264 T296
BS03 ATP K R49 N51 H54 R90 R175 S330 R49 N51 H54 R90 R175 S330
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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Cellular Component
External links
PDB RCSB:3hqo, PDBe:3hqo, PDBj:3hqo
PDBsum3hqo
PubMed20123988
UniProtQ27686|KPYK_LEIME Pyruvate kinase (Gene Name=PYK)

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