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Crystal structure of a constitutively activated rhoa mutant (Q63L)

Analyse Crystal structure of a constitutively activated rhoa mutant (Q63L) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1KMQ
Type: protein
Length: 177 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transforming protein rhoa
UniProt: P61586
Ligands: GNP, MG
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transforming protein rhoa	protein	177	40% helix, 25% strand	P61586

Ligands and binding sites

GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
MG · Magnesium ion · metal · 2 copies · chains A
DIO · 1,4-diethylene dioxide · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	145	0.56	0.82	30	MG, GNP

Compared structures

1KMQ · Crystal Structure of a Constitutively Activated RhoA Mutant (Q63L) · the same entry in another collection · chain A against A, TM-score 1.00
P61586 · AlphaFold monomer V2.0 prediction for transforming protein rhoa (P61586) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P61586
Elsewhere: RCSB PDB 1KMQ · PDBe 1KMQ · UniProt P61586

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