Structure of PDB 4kcw Chain B

Receptor sequence
>4kcwB (length=498) Species: 5702 (Trypanosoma brucei brucei) [Search protein sequence]
SQLEHNIGLSIFEPVAKHRANRIVCTIGPSTQSVEALKNLMKSGMSVARM
NFSHGSHEYHQTTINNVRAAAAELGLHIGIALDTKGPEIRTGLFKDGEVS
FAPGDIVCVTTDPAYEKVGTKEKFYIDYPQLTNAVRPGGSIYVDDGVMTL
RVVSKEDDRTLKCHVNNHHRLTDRRGINLPGCEVDLPAVSEKDRKDLEFG
VAQGVDMIFASFIRTAEQVREVRAALGEKGKDILIISKIENHQGVQNIDS
IIEASNGIMVARGDLGVEIPAEKVCVAQMCIISKCNVVGKPVICATQMLE
SMTSNPRPTRAEVSDVANAVLNGADCVMLSGETAKGKYPNEVVQYMARIC
VEAQSATHDTVMFNSIKNLQKIPMCPEEAVCSSAVASAFEVQAKAMLVLS
NTGRSARLISKYRPNCPIICVTTRLQTCRQLNVTRSVVSVFYDAAKSGED
KDKEKRVKLGLDFAKKEKYASTGDVVVVVHADHSVKGYPNQTRLIYLP
3D structure
PDB4kcw Pyruvate kinases have an intrinsic and conserved decarboxylase activity.
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 B E241 D265 E240 D264
BS02 OXL B K239 E241 A262 G264 D265 T297 K238 E240 A261 G263 D264 T296
BS03 FDP B 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4kcw, PDBe:4kcw, PDBj:4kcw
PDBsum4kcw
PubMed24328825
UniProtP30615|KPYK1_TRYBB Pyruvate kinase 1 (Gene Name=PYK1)

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