Structure of PDB 5scc Chain E

Receptor sequence
>5sccE (length=419) Species: 9606 (Homo sapiens) [Search protein sequence]
AFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVER
LKEMIKAGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPVAI
ALDTKGPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAALGPEG
HGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKM
MIGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLS
GETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVT
AIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIAVTRSAQAARQ
VHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGDLVIVV
TGWRPGSGYTNIMRVLSIS
3D structure
PDB5scc Anthraquinone derivatives as ADP-competitive inhibitors of liver pyruvate kinase.
ChainE
Resolution1.885 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 E L443 T444 T445 T446 S449 W494 R501 G526 R528 G530 S531 Y533 T534 L319 T320 T321 T322 S325 W370 R377 G402 R404 G406 S407 Y409 T410
BS02 OXL E K282 E284 A305 G307 D308 T340 K158 E160 A181 G183 D184 T216
BS03 MG E E284 D308 E160 D184
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:5scc, PDBe:5scc, PDBj:5scc
PDBsum5scc
PubMed35290845
UniProtP30613|KPYR_HUMAN Pyruvate kinase PKLR (Gene Name=PKLR)

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