Structure of PDB 4hyv Chain A

Receptor sequence

>4hyvA (length=498) Species: 5702 (Trypanosoma brucei brucei)

SQLEHNIGLSIFEPVAKHRANRIVCTIGPSTQSVEALKNLMKSGMSVARM
NFSHGSHEYHQTTINNVRAAAAELGLHIGIALDTKGPEIRTGLFKDGEVS
FAPGDIVCVTTDPAYEKVGTKEKFYIDYPQLTNAVRPGGSIYVDDGVMTL
RVVSKEDDRTLKCHVNNHHRLTDRRGINLPGCEVDLPAVSEKDRKDLEFG
VAQGVDMIFASFIRTAEQVREVRAALGEKGKDILIISKIENHQGVQNIDS
IIEASNGIMVARGDLGVEIPAEKVCVAQMCIISKCNVVGKPVICATQMLE
SMTSNPRPTRAEVSDVANAVLNGADCVMLSGETAKGKYPNEVVQYMARIC
VEAQSATHDTVMFNSIKNLQKIPMCPEEAVCSSAVASAFEVQAKAMLVLS
NTGRSARLISKYRPNCPIICVTTRLQTCRQLNVTRSVVSVFYDAAKSGED
KDKEKRVKLGLDFAKKEKYASTGDVVVVVHADHSVKGYPNQTRLIYLP

3D structure

• PDB: 4hyv `In crystallo' substrate binding triggers major domain movements and reveals magnesium as a co-activator of Trypanosoma brucei pyruvate kinase.
• Chain: A
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R50 R91 K239 T297
• 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	MG	A	E241 D265	E240 D264
BS02	PEP	A	R50 K239 E241 A262 G264 D265 T297	R49 K238 E240 A261 G263 D264 T296
BS03	FDP	A	L400 S401 N402 T403 S406 K454 R457 H481 A482 K487 G488 Y489	L399 S400 N401 T402 S405 K453 R456 H480 A481 K486 G487 Y488

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:4hyv, PDBe:4hyv, PDBj:4hyv
• PDBsum: 4hyv
• PubMed: 23999300
• UniProt: P30615|KPYK1_TRYBB Pyruvate kinase 1 (Gene Name=PYK1)