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Crystal structure of rhogdi E154A,E155A mutant

Analyse Crystal structure of rhogdi E154A,E155A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2JHU
Type: protein
Length: 276 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rho GDP-dissociation inhibitor 1
UniProt: P52565
Ligands: SO4
Pockets: 3 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Rho GDP-dissociation inhibitor 1	protein	138	7% helix, 56% strand	P52565

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	281	0.61	0.79	41	empty
2	122	0.47	0.78	19	empty
3	73	0.40	0.79	16	empty

Interfaces

1 interface between chains.

A–B · 565 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

2JHU · Crystal structure of rhogdi E154A,E155A mutant · the same entry in another collection · chain A against A, TM-score 1.00
P52565 · AlphaFold monomer V2.0 prediction for rho GDP-dissociation inhibitor 1 (P52565) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 P52565
Elsewhere: RCSB PDB 2JHU · PDBe 2JHU · UniProt P52565

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