Structure of PDB 5sck Chain A

Receptor sequence
>5sckA (length=418) Species: 9606 (Homo sapiens) [Search protein sequence]
QQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKE
MIKAGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPVAIALD
TKGPGSGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAALGPEGH
GIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMM
IGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSG
ETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTA
IGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIAVTRSAQAARQV
HLCRGVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGDLVIVVT
GWRPGSGYTNIMRVLSIS
3D structure
PDB5sck Anthraquinone derivatives as ADP-competitive inhibitors of liver pyruvate kinase.
ChainA
Resolution1.717 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 A L443 T444 T445 T446 S449 W494 R501 G526 R528 P529 G530 S531 G532 Y533 T534 L318 T319 T320 T321 S324 W369 R376 G401 R403 P404 G405 S406 G407 Y408 T409
BS02 OXL A K282 E284 A305 G307 D308 T340 K157 E159 A180 G182 D183 T215
BS03 MG A E284 D308 E159 D183
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:5sck, PDBe:5sck, PDBj:5sck
PDBsum5sck
PubMed35290845
UniProtP30613|KPYR_HUMAN Pyruvate kinase PKLR (Gene Name=PKLR)

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