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Crystal structure of the DH/PH domains of P115-rhogef

Analyse Crystal structure of the DH/PH domains of P115-rhogef in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ODO
Type: protein
Length: 740 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rho guanine nucleotide exchange factor 1
UniProt: Q92888
Pockets: 6 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Rho guanine nucleotide exchange factor 1	protein	370	55% helix, 15% strand	Q92888

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	144	0.62	0.85	19	empty
2	92	0.58	0.87	20	empty
3	159	0.43	0.75	24	empty
4	140	0.41	0.74	20	empty
5	81	0.34	0.75	15	empty

Interfaces

1 interface between chains.

A–B · 900 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

3ODO · Crystal Structure of the DH/PH Domains of p115-RhoGEF · the same entry in another collection · chain A against A, TM-score 1.00
Q92888 · AlphaFold monomer V2.0 prediction for rho guanine nucleotide exchange factor 1 (Q92888) · a predicted model of the same protein · chain B against A, TM-score 0.96

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 Q92888
Elsewhere: RCSB PDB 3ODO · PDBe 3ODO · UniProt Q92888

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