Structure of PDB 5sci Chain D

Receptor sequence
>5sciD (length=425) Species: 9606 (Homo sapiens) [Search protein sequence]
GTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSV
ERLKEMIKAGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPV
AIALDTKGPGSGPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRA
ALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKV
FLAQKMMIGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGA
DCIMLSGETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSR
DPTEVTAIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIAVTRS
AQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVG
DLVIVVTGWRPGSGYTNIMRVLSIS
3D structure
PDB5sci Anthraquinone derivatives as ADP-competitive inhibitors of liver pyruvate kinase.
ChainD
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 D T444 T445 T446 S449 W494 R501 G526 R528 P529 G530 S531 G532 Y533 T534 T326 T327 T328 S331 W376 R383 G408 R410 P411 G412 S413 G414 Y415 T416
BS02 OXL D K282 E284 A305 G307 D308 T340 K164 E166 A187 G189 D190 T222
BS03 MG D 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:5sci, PDBe:5sci, PDBj:5sci
PDBsum5sci
PubMed35290845
UniProtP30613|KPYR_HUMAN Pyruvate kinase PKLR (Gene Name=PKLR)

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