Structure of PDB 5sch Chain A

Receptor sequence
>5schA (length=417) Species: 9606 (Homo sapiens) [Search protein sequence]
QQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKE
MIKAGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPVAIALD
TKGPGSLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAALGPEGHG
IKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMI
GRCNLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGE
TAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAI
GAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIAVTRSAQAARQVH
LCRGVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGDLVIVVTG
WRPGSGYTNIMRVLSIS
3D structure
PDB5sch Anthraquinone derivatives as ADP-competitive inhibitors of liver pyruvate kinase.
ChainA
Resolution2.089 Å
3D
structure
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Enzymatic activity
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 FBP A L443 T444 T445 T446 S449 W494 R501 G526 R528 P529 G530 S531 G532 Y533 T534 L317 T318 T319 T320 S323 W368 R375 G400 R402 P403 G404 S405 G406 Y407 T408
BS02 OXL A K282 E284 A305 G307 D308 T340 K156 E158 A179 G181 D182 T214
BS03 MG A E284 D308 E158 D182
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0004743 pyruvate kinase activity
GO:0030955 potassium ion binding
Biological Process
GO:0006096 glycolytic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5sch, PDBe:5sch, PDBj:5sch
PDBsum5sch
PubMed35290845
UniProtP30613|KPYR_HUMAN Pyruvate kinase PKLR (Gene Name=PKLR)

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