Structure of PDB 3n25 Chain A

Receptor sequence
>3n25A (length=519) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
IQTQQLHAAMADTFLEHKCRLDIDSAPITARNTGIICTIGPASRSVETLK
EMIKSGMNVARMNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVAL
DTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYK
NICKVVDVGSKVYVDDGLISLQVKQKGPDFLVTEVENGGFLGSKKGVNLP
GAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKAADVHEVRKILGEKG
KNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKM
IIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLS
GETAKGDYPLEAVRMQHLIAREAEAAMFHRKLFEELARASSQSTDLMEAM
AMGSVEASYKCLAAALIVLTESGRSAHQVARYRPRAPIIAVTRNHQTARQ
AHLYRGIFPVVCKDPVQEAWAEDVDLRVNLAMNVGKARGFFKKGDVVIVL
TGWRPGSGFTNTMRVVPVP
3D structure
PDB3n25 The pyruvate kinase model system, a cautionary tale for the use of osmolyte perturbations to support conformational equilibria in allostery.
ChainA
Resolution2.41 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R72 R119 K269 T327
Catalytic site (residue number reindexed from 1) R61 R108 K258 T316
Enzyme Commision number 2.7.10.2: non-specific protein-tyrosine kinase.
2.7.11.1: non-specific serine/threonine protein kinase.
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 PRO A N43 N69 H463 I468 F469 N32 N58 H452 I457 F458
BS02 MN A E271 D295 E260 D284
BS03 PYR A K269 E271 A292 G294 D295 T327 K258 E260 A281 G283 D284 T316
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003729 mRNA binding
GO:0003824 catalytic activity
GO:0004713 protein tyrosine kinase activity
GO:0004743 pyruvate kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0030955 potassium ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006096 glycolytic process
GO:0006417 regulation of translation
GO:0016310 phosphorylation
GO:0032869 cellular response to insulin stimulus
GO:1903672 positive regulation of sprouting angiogenesis
GO:2000767 positive regulation of cytoplasmic translation
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005791 rough endoplasmic reticulum

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3n25, PDBe:3n25, PDBj:3n25
PDBsum3n25
PubMed20629175
UniProtP11974|KPYM_RABIT Pyruvate kinase PKM (Gene Name=PKM)

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