Structure of PDB 3qv7 Chain B

Receptor sequence

>3qv7B (length=400) Species: 5665 (Leishmania mexicana)

SQLAHNLTLSIFDPVANYRAARIICTIGPSTQSVEALKGLIQSGMSVARM
NFSHGSHEYHQTTINNVRQAAAELGVNIAIALDTKGPLPAVSAKDRVDLQ
FGVEQGVDMIFASFIRSAEQVGDVRKALGPKGRDIMIICKIENHQGVQNI
DSIIEESDGIMVARGDLGVEIPAEKVVVAQKILISKCNVAGKPVICATQM
LESMTYNPRPTRAEVSDVANAVFNGADCVMLSGETAKGKYPNEVVQYMAR
ICLEAQSALNEYVFFNSIKKLQHIPMSADEAVCSSAVNSVYETKAKAMVV
LSNTGRSARLVAKYRPNCPIVCVTTRLQTCRQLNITQGVESVFFDADKLG
HDEGKEHRVAAGVEFAKSKGYVQTGDYCVVIHADHKVKGYANQTRILLVE

3D structure

• PDB: 3qv7 The trypanocidal drug suramin and other trypan blue mimetics are inhibitors of pyruvate kinases and bind to the adenosine site.
• Chain: B
• Resolution: 2.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R49 K238 T296
• Catalytic site (residue number reindexed from 1): R49 K140 T198
• 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	QV7	B	T402 R404 D482 H483 V485 K486	T304 R306 D384 H385 V387 K388
BS02	QV8	B	R231 D232 R424	R133 D134 R326
BS03	QV7	B	S1 Y360 V361 N364	S1 Y262 V263 N266

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:3qv7, PDBe:3qv7, PDBj:3qv7
• PDBsum: 3qv7
• PubMed: 21733839
• UniProt: Q27686|KPYK_LEIME Pyruvate kinase (Gene Name=PYK)