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Crystal structure of human TTC5 (strap) C-terminal ob domain

Analyse Crystal structure of human TTC5 (strap) C-terminal ob domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2XVS
Type: protein
Length: 166 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tetratricopeptide repeat protein 5
UniProt: Q8N0Z6
Ligands: IOD, CL
Pockets: 2 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tetratricopeptide repeat protein 5	protein	166	27% helix, 35% strand	Q8N0Z6

Ligands and binding sites

IOD · Iodide ion · ion · 3 copies · chains A
CL · Chloride ion · ion · chains A
EDO · 1,2-ethanediol · additive · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	61	0.37	0.78	14	empty
2	66	0.30	0.74	15	empty

Compared structures

2XVS · Crystal structure of human TTC5 (Strap) C-terminal OB domain · the same entry in another collection · chain A against A, TM-score 1.00
Q8N0Z6 · AlphaFold monomer V2.0 prediction for tetratricopeptide repeat protein 5 (Q8N0Z6) · a predicted model of the same protein · chain A 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 Q8N0Z6
Elsewhere: RCSB PDB 2XVS · PDBe 2XVS · UniProt Q8N0Z6

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