Structure of PDB 3n25 Chain E

Receptor sequence
>3n25E (length=521) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
AFIQTQQLHAAMADTFLEHKCRLDIDSAPITARNTGIICTIGPASRSVET
LKEMIKSGMNVARMNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAV
ALDTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLD
YKNICKVVDVGSKVYVDDGLISLQVKQKGPDFLVTEVENGGFLGSKKGVN
LPGAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKAADVHEVRKILGE
KGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQ
KMIIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIM
LSGETAKGDYPLEAVRMQHLIAREAEAAMFHRKLFEELARASSQSTDLME
AMAMGSVEASYKCLAAALIVLTESGRSAHQVARYRPRAPIIAVTRNHQTA
RQAHLYRGIFPVVCKDPVQEAWAEDVDLRVNLAMNVGKARGFFKKGDVVI
VLTGWRPGSGFTNTMRVVPVP
3D structure
PDB3n25 The pyruvate kinase model system, a cautionary tale for the use of osmolyte perturbations to support conformational equilibria in allostery.
ChainE
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) R63 R110 K260 T318
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 E N43 N69 H463 I468 F469 N34 N60 H454 I459 F460
BS02 MN E E271 D295 E262 D286
BS03 PYR E K269 E271 A292 G294 D295 T327 K260 E262 A283 G285 D286 T318
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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