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Crystal structure of EHRHO1 bound to a GTP analog and magnesium

Analyse Crystal structure of EHRHO1 bound to a GTP analog and magnesium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3REG
Type: protein
Length: 339 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rho-like small GTPase
UniProt: Q95TD4
Ligands: GSP, MG
Pockets: 3 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Rho-like small GTPase	protein	171	36% helix, 27% strand	Q95TD4
B	Rho-like small GTPase	protein	168	38% helix, 27% strand	Q95TD4

Ligands and binding sites

GSP · 5'-guanosine-diphosphate-monothiophosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	138	0.56	0.82	30	GSP, MG
2	314	0.55	0.75	52	empty
3	152	0.54	0.80	33	GSP, MG

Interfaces

1 interface between chains.

A–B · 458 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

3REG · Crystal structure of EhRho1 bound to a GTP analog and Magnesium · the same entry in another collection · chain A against A, TM-score 1.00

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 Q95TD4
Elsewhere: RCSB PDB 3REG · PDBe 3REG · UniProt Q95TD4

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