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Crystal structure of rhogdi GLU(154,155)ALA mutant

Analyse Crystal structure of rhogdi GLU(154,155)ALA mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1KMT
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
Pockets: 3 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Rho GDP-dissociation inhibitor 1	protein	138	4% helix, 57% strand	P52565

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	94	0.51	0.82	18	empty
2	89	0.48	0.81	19	empty
3	68	0.30	0.74	15	empty

Interfaces

1 interface between chains.

A–B · 597 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

1KMT · Crystal structure of RhoGDI Glu(154,155)Ala 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 1KMT · PDBe 1KMT · UniProt P52565

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