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Crystal structure of the DH/PH domains of leukemia-associated rhogef

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

PDB: 1TXD
Type: protein
Length: 352 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rho guanine nucleotide exchange factor 12
UniProt: Q9NZN5
Pockets: 1 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 62% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Rho guanine nucleotide exchange factor 12	protein	352	62% helix, 15% strand	Q9NZN5

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	82	0.32	0.74	15	empty

Compared structures

1TXD · Crystal Structure of the DH/PH domains of Leukemia-associated RhoGEF · the same entry in another collection · chain A against A, TM-score 1.00
Q9NZN5 · AlphaFold monomer V2.0 prediction for rho guanine nucleotide exchange factor 12 (Q9NZN5) · a predicted model of the same protein · chain A against A, TM-score 0.80

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 Q9NZN5
Elsewhere: RCSB PDB 1TXD · PDBe 1TXD · UniProt Q9NZN5

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