Structure of PDB 7qdn Chain B

Receptor sequence
>7qdnB (length=436) Species: 9606 (Homo sapiens) [Search protein sequence]
RADVAQLTQELGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSI
IATIGPASRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVREAVES
FAGSPLSYRPVAIALDTKGPGSGPGLSEQDVRDLRFGVEHGVDIVFASFV
RKASDVAAVRAALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARG
DLGIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQMLESMITKPRPTRAET
SDVANAVLDGADCIMLSGETAKGNFPVEAVKMQHAIAREAEAAVYHRQLF
EELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYR
PRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIE
SGKLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS
3D structure
PDB7qdn Anthraquinone derivatives as ADP-competitive inhibitors of liver pyruvate kinase.
ChainB
Resolution1.695 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 B L443 T444 T445 T446 S449 W494 R501 G526 R528 P529 G530 S531 G532 Y533 T534 L336 T337 T338 T339 S342 W387 R394 G419 R421 P422 G423 S424 G425 Y426 T427
BS02 OXD B K282 E284 A305 G307 D308 T340 K175 E177 A198 G200 D201 T233
BS03 MG B E284 D308 E177 D201
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:7qdn, PDBe:7qdn, PDBj:7qdn
PDBsum7qdn
PubMed35290845
UniProtP30613|KPYR_HUMAN Pyruvate kinase PKLR (Gene Name=PKLR)

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