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Structural genomics, crystal structure of the chex protein from thermotoga maritima

Analyse Structural genomics, crystal structure of the chex protein from thermotoga… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1SQU
Type: protein
Length: 306 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chex protein
UniProt: Q9X1V3
Pockets: 2 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chex protein	protein	152	34% helix, 30% strand	Q9X1V3
B	Chex protein	protein	154	34% helix, 32% strand	Q9X1V3

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	53	0.73	0.99	17	empty
2	87	0.35	0.75	18	empty

Interfaces

1 interface between chains.

A–B · 1310 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

1SQU · Structural Genomics, Crystal structure of the CheX protein from Thermotoga maritima · the same entry in another collection · chain A against A, TM-score 1.00
Q9X1V3 · AlphaFold monomer V2.0 prediction for chey-P phosphatase chex (Q9X1V3) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 Q9X1V3
Elsewhere: RCSB PDB 1SQU · PDBe 1SQU · UniProt Q9X1V3

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