Structure of PDB 5sci Chain B

Receptor sequence
>5sciB (length=435) Species: 9606 (Homo sapiens) [Search protein sequence]
RADVAQLTQELGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSI
IATIGPASRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVREAVES
FAGSPLSYRPVAIALDTKGPGSPGLSEQDVRDLRFGVEHGVDIVFASFVR
KASDVAAVRAALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGD
LGIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQMLESMITKPRPTRAETS
DVANAVLDGADCIMLSGETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFE
ELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRP
RAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIES
GKLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS
3D structure
PDB5sci Anthraquinone derivatives as ADP-competitive inhibitors of liver pyruvate kinase.
ChainB
Resolution2.155 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 L443 T444 T445 T446 S449 W494 R501 G526 R528 G530 S531 Y533 T534 L335 T336 T337 T338 S341 W386 R393 G418 R420 G422 S423 Y425 T426
BS02 OXL B K282 E284 A305 G307 D308 T340 K174 E176 A197 G199 D200 T232
BS03 MG B E284 D308 E176 D200
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:5sci, PDBe:5sci, PDBj:5sci
PDBsum5sci
PubMed35290845
UniProtP30613|KPYR_HUMAN Pyruvate kinase PKLR (Gene Name=PKLR)

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