Structure of PDB 4ks0 Chain A

Receptor sequence
>4ks0A (length=466) Species: 353153 (Trypanosoma cruzi strain CL Brener) [Search protein sequence]
MSQLAHNVNLSIFEPISHHRANRIVCTIGPSTQSVEALKGLIRSGMSVAR
MNFSHGSHEYHQTTINNLRAAATELGAHIGLALDTKGPEIRTYIEYPRLS
ITVRPGGFIYIDDGVLSLKVLSKEDEYTLKCYVNNAHFLTDRKGCNLPGC
EVDLPAVSEKDREDLKFGVEQGIDMVFASFIRTAEQVQEVREALGEKGKD
ILIISKIENHQGVQNIDGIIEASDGIMVARGDLGVEIPAEKVVVAQMILI
SKCNVAGKPVICATQMLESMTTNPRPTRAEVSDVANAVFNGADCVMLSGE
TAKGKYPNEVVQYMARICLEAQSATNQAVMFNSIKKMQKLPMSPEEAVCS
SAVNSVYEVRAKALLVLSNSGRSARLASKYRPDCPIICATTRMRTCRQLT
ITRSVDAVFYDAERYGEDENKEKRVQLGVDCAKKKGYVVPGDLMVVVHAD
HKVKGYPNQTRIIYVS
3D structure
PDB4ks0 Structures of pyruvate kinases display evolutionarily divergent allosteric strategies.
ChainA
Resolution2.8 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) R50 R91 K206 T264
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 E208 D232
BS02 OXL A K239 E241 A262 R263 G264 D265 T297 K206 E208 A229 R230 G231 D232 T264
BS03 FDP A L400 S401 N402 S403 R405 S406 K454 R457 H481 A482 K487 G488 Y489 L367 S368 N369 S370 R372 S373 K421 R424 H448 A449 K454 G455 Y456
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:0016491 oxidoreductase 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:4ks0, PDBe:4ks0, PDBj:4ks0
PDBsum4ks0
PubMed26064527
UniProtQ4D9Z4

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