Structure of PDB 5scb Chain H

Receptor sequence
>5scbH (length=425) Species: 9606 (Homo sapiens) [Search protein sequence]
GTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSV
ERLKEMIKAGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPV
AIALDTKGPGSGPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRA
ALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKV
FLAQKMMIGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGA
DCIMLSGETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSR
DPTEVTAIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIAVTRS
AQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVG
DLVIVVTGWRPGSGYTNIMRVLSIS
3D structure
PDB5scb Anthraquinone derivatives as ADP-competitive inhibitors of liver pyruvate kinase.
ChainH
Resolution1.8 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 L325 T326 T327 T328 S331 W376 R383 G408 R410 P411 G412 S413 G414 Y415 T416
BS02 OXL H K282 E284 A305 G307 D308 T340 K164 E166 A187 G189 D190 T222
BS03 MG H E284 D308 E166 D190
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:5scb, PDBe:5scb, PDBj:5scb
PDBsum5scb
PubMed35290845
UniProtP30613|KPYR_HUMAN Pyruvate kinase PKLR (Gene Name=PKLR)

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