Structure of PDB 4lyh Chain B

Receptor sequence
>4lyhB (length=159) Species: 9606 (Homo sapiens) [Search protein sequence]
MTEYKLVVVGACGVGKSALTIQLIQNHFVYRKQVVIDGETSLLDILDTAG
QEEYSAMRDQYMRTGEGFLLVFAINNTKSFEDIHHYREQIKRVKDSEDVP
MVLVGNKSDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTLV
REIRKHKEK
3D structure
PDB4lyh K-Ras(G12C) inhibitors allosterically control GTP affinity and effector interactions.
ChainB
Resolution1.371 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 21F B V9 G10 C12 T58 E62 R68 Y96 V9 G10 C12 T48 E52 R58 Y86
BS02 GDP B G13 G15 K16 S17 A18 F28 N116 K117 D119 S145 A146 G13 G15 K16 S17 A18 F28 N106 K107 D109 S135 A136
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:4lyh, PDBe:4lyh, PDBj:4lyh
PDBsum4lyh
PubMed24256730
UniProtP01116|RASK_HUMAN GTPase KRas (Gene Name=KRAS)

[Back to BioLiP]