Structure of PDB 5sce Chain A

Receptor sequence
>5sceA (length=418) Species: 9606 (Homo sapiens) [Search protein sequence]
QQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKE
MIKAGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPVAIALD
TKGPGSGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAALGPEGH
GIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMM
IGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSG
ETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTA
IGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIAVTRSAQAARQV
HLCRGVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGDLVIVVT
GWRPGSGYTNIMRVLSIS
3D structure
PDB5sce Anthraquinone derivatives as ADP-competitive inhibitors of liver pyruvate kinase.
ChainA
Resolution2.147 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 T444 T445 T446 S449 W494 R501 G526 R528 P529 G530 S531 G532 Y533 T319 T320 T321 S324 W369 R376 G401 R403 P404 G405 S406 G407 Y408
BS02 OXL A K282 E284 A305 G307 D308 T340 K157 E159 A180 G182 D183 T215
BS03 MG A E284 D308 E159 D183
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:5sce, PDBe:5sce, PDBj:5sce
PDBsum5sce
PubMed35290845
UniProtP30613|KPYR_HUMAN Pyruvate kinase PKLR (Gene Name=PKLR)

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