Structure of PDB 5sdt Chain H

Receptor sequence
>5sdtH (length=429) Species: 9606 (Homo sapiens) [Search protein sequence]
TQELGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPA
SRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLS
YRPVAIALDTKGPGSGPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVA
AVRAALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIP
AEKVFLAQKMMIGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVANAV
LDGADCIMLSGETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRRAA
PLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIA
VTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGF
LRVGDLVIVVTGWRPGSGYTNIMRVLSIS
3D structure
PDB5sdt Anthraquinone derivatives as ADP-competitive inhibitors of liver pyruvate kinase.
ChainH
Resolution1.944 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 L329 T330 T331 T332 S335 W380 R387 G412 R414 P415 G416 S417 G418 Y419 T420
BS02 OXL H K282 E284 A305 G307 D308 T340 K168 E170 A191 G193 D194 T226
BS03 MG H E284 D308 E170 D194
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:5sdt, PDBe:5sdt, PDBj:5sdt
PDBsum5sdt
PubMed35290845
UniProtP30613|KPYR_HUMAN Pyruvate kinase PKLR (Gene Name=PKLR)

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