Structure of PDB 5sci Chain A

Receptor sequence
>5sciA (length=422) Species: 9606 (Homo sapiens) [Search protein sequence]
AFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVER
LKEMIKAGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPVAI
ALDTKGPGSGGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAALG
PEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLA
QKMMIGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCI
MLSGETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPT
EVTAIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIAVTRSAQA
ARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGDLV
IVVTGWRPGSGYTNIMRVLSIS
3D structure
PDB5sci Anthraquinone derivatives as ADP-competitive inhibitors of liver pyruvate kinase.
ChainA
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 A L443 T444 T445 T446 S449 W494 R501 G526 R528 P529 G530 S531 G532 Y533 T534 L322 T323 T324 T325 S328 W373 R380 G405 R407 P408 G409 S410 G411 Y412 T413
BS02 OXL A K282 E284 A305 G307 D308 T340 K161 E163 A184 G186 D187 T219
BS03 MG A E284 D308 E163 D187
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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