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Crystal structure of dh-pH domain of RHOGEF3(XPLN)

Analyse Crystal structure of dh-pH domain of RHOGEF3(XPLN) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2Z0Q
Type: protein
Length: 321 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rho guanine nucleotide exchange factor 3
UniProt: Q91X46
Ligands: SO4
Pockets: 2 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 57% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Rho guanine nucleotide exchange factor 3	protein	321	57% helix, 16% strand	Q91X46

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A

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

Pockets

2 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	198	0.52	0.78	23	empty
2	205	0.48	0.75	29	empty

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

2Z0Q · Crystal structure of DH-PH domain of RhoGEF3(Xpln) · the same entry in another collection · chain A against A, TM-score 1.00
Q91X46 · AlphaFold monomer V2.0 prediction for rho guanine nucleotide exchange factor 3 (Q91X46) · a predicted model of the same protein · chain A against A, TM-score 0.82

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 Q91X46
Elsewhere: RCSB PDB 2Z0Q · PDBe 2Z0Q · UniProt Q91X46

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