Structure of PDB 3hqq Chain V

Receptor sequence

>3hqqV (length=498) Species: 5665 (Leishmania mexicana)

SQLAHNLTLSIFDPVANYRAARIICTIGPSTQSVEALKGLIQSGMSVARM
NFSHGSHEYHQTTINNVRQAAAELGVNIAIALDTKGPEIRTGQFVGGDAV
MERGATCYVTTDPAFADKGTKDKFYIDYQNLSKVVRPGNYIYIDDGILIL
QVQSHEDEQTLECTVTNSHTISDRRGVNLPGCDVDLPAVSAKDRVDLQFG
VEQGVDMIFASFIRSAEQVGDVRKALGPKGRDIMIICKIENHQGVQNIDS
IIEESDGIMVARGDLGVEIPAEKVVVAQKILISKCNVAGKPVICATQMLE
SMTYNPRPTRAEVSDVANAVFNGADCVMLSGETAKGKYPNEVVQYMARIC
LEAQSALNEYVFFNSIKKLQHIPMSADEAVCSSAVNSVYETKAKAMVVLS
NTGRSARLVAKYRPNCPIVCVTTRLQTCRQLNITQGVESVFFDADKLGHD
EGKEHRVAAGVEFAKSKGYVQTGDYCVVIHADHKVKGYANQTRILLVE

3D structure

• PDB: 3hqq The allosteric mechanism of pryuvate kinase from Leishmania mexicana: a rock and lock model
• Chain: V
• Resolution: 5.07 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R49 R90 K238 T296
• Catalytic site (residue number reindexed from 1): R49 R90 K238 T296
• 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	FDP	V	L399 S400 N401 T402 S405 K453 R456 H480 A481	L399 S400 N401 T402 S405 K453 R456 H480 A481

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

External links

• PDB: RCSB:3hqq, PDBe:3hqq, PDBj:3hqq
• PDBsum: 3hqq
• PubMed: 20123988
• UniProt: Q27686|KPYK_LEIME Pyruvate kinase (Gene Name=PYK)