Structure of PDB 1aqf Chain F

Receptor sequence
>1aqfF (length=519) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
IQTQQLHAAMADTFLEHMCRLDIDSAPITARNTGIICTIGPASRSVETLK
EMIKSGMNVARMNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVAL
DTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYK
NICKVVDVGSKVYVDDGLISLQVKQKGPDFLVTEVENGGFLGSKKGVNLP
GAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKAADVHEVRKILGEKG
KNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKM
IIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLS
GETAKGDYPLEAVRMQHLIAREAEAAMFHRKLFEELARSSSHSTDLMEAM
AMGSVEASYKCLAAALIVLTESGRSAHQVARYRPRAPIIAVTRNHQTARQ
AHLYRGIFPVVCKDPVQEAWAEDVDLRVNLAMNVGKARGFFKKGDVVIVL
TGWRPGSGFTNTMRVVPVP
3D structure
PDB1aqf Ligand-induced domain movement in pyruvate kinase: structure of the enzyme from rabbit muscle with Mg2+, K+, and L-phospholactate at 2.7 A resolution.
ChainF
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 MG F E271 D295 E260 D284
BS02 PEQ F R72 K269 A292 G294 D295 T327 R61 K258 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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1aqf, PDBe:1aqf, PDBj:1aqf
PDBsum1aqf
PubMed9308890
UniProtP11974|KPYM_RABIT Pyruvate kinase PKM (Gene Name=PKM)

[Back to BioLiP]