Structure of PDB 5sc9 Chain B

Receptor sequence
>5sc9B (length=431) Species: 9606 (Homo sapiens) [Search protein sequence]
DVAQLTQELGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIA
TIGPASRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVREAVESFA
GSPLSYRPVAIALDTKGPPGLSEQDVRDLRFGVEHGVDIVFASFVRKASD
VAAVRAALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIE
IPAEKVFLAQKMMIGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVAN
AVLDGADCIMLSGETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRR
AAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAV
IAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESGKLR
GFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS
3D structure
PDB5sc9 Anthraquinone derivatives as ADP-competitive inhibitors of liver pyruvate kinase.
ChainB
Resolution1.685 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 B T444 T445 T446 S449 W494 R501 G526 R528 G530 S531 G532 Y533 T534 T332 T333 T334 S337 W382 R389 G414 R416 G418 S419 G420 Y421 T422
BS02 OXL B K282 E284 A305 G307 D308 T340 K170 E172 A193 G195 D196 T228
BS03 MG B E284 D308 E172 D196
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:5sc9, PDBe:5sc9, PDBj:5sc9
PDBsum5sc9
PubMed35290845
UniProtP30613|KPYR_HUMAN Pyruvate kinase PKLR (Gene Name=PKLR)

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