Structure of PDB 4lv6 Chain A

Receptor sequence
>4lv6A (length=168) Species: 9606 (Homo sapiens) [Search protein sequence]
MTEYKLVVVGACGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGET
SLLDILDTAGQEEYSAMRDQYMRTGEGFLLVFAINNTKSFEDIHHYREQI
KRVKDSEDVPMVLVGNKSDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQ
GVDDAFYTLVREIRKHKE
3D structure
PDB4lv6 K-Ras(G12C) inhibitors allosterically control GTP affinity and effector interactions.
ChainA
Resolution1.5 Å
3D
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
Enzyme Commision number 3.6.5.2: small monomeric GTPase.
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 20H A V9 G10 C12 A59 G60 Q61 R68 M72 Y96 I100 V9 G10 C12 A59 G60 Q61 R68 M72 Y96 I100
BS02 GDP A G13 G15 K16 S17 A18 F28 D30 N116 K117 D119 L120 S145 A146 K147 G13 G15 K16 S17 A18 F28 D30 N116 K117 D119 L120 S145 A146 K147
Gene Ontology
Molecular Function
GO:0003924 GTPase activity
GO:0005525 GTP binding
Biological Process
GO:0007165 signal transduction
Cellular Component
GO:0016020 membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4lv6, PDBe:4lv6, PDBj:4lv6
PDBsum4lv6
PubMed24256730
UniProtP01116|RASK_HUMAN GTPase KRas (Gene Name=KRAS)

[Back to BioLiP]