Structure of PDB 5scc Chain H

Receptor sequence
>5sccH (length=424) Species: 9606 (Homo sapiens) [Search protein sequence]
GTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSV
ERLKEMIKAGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPV
AIALDTKGPGSGPLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAA
LGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVF
LAQKMMIGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGAD
CIMLSGETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRD
PTEVTAIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIAVTRSA
QAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGD
LVIVVTGWRPGSGYTNIMRVLSIS
3D structure
PDB5scc Anthraquinone derivatives as ADP-competitive inhibitors of liver pyruvate kinase.
ChainH
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 H L443 T444 T445 T446 S449 W494 R501 G526 R528 P529 G530 S531 G532 Y533 T534 L324 T325 T326 T327 S330 W375 R382 G407 R409 P410 G411 S412 G413 Y414 T415
BS02 OXL H K282 E284 A305 G307 D308 T340 K163 E165 A186 G188 D189 T221
BS03 MG H E284 D308 E165 D189
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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