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Crystal structure of human THEM5

Analyse Crystal structure of human THEM5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4AE7
Type: protein
Length: 186 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioesterase superfamily member 5
UniProt: Q8N1Q8
Pockets: 2 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioesterase superfamily member 5	protein	186	23% helix, 34% strand	Q8N1Q8

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	106	0.53	0.82	20	empty
2	53	0.28	0.74	12	empty

Compared structures

4AE7 · Crystal structure of human THEM5 · the same entry in another collection · chain A against A, TM-score 1.00
Q8N1Q8 · AlphaFold monomer V2.0 prediction for acyl-coenzyme a thioesterase THEM5 (Q8N1Q8) · a predicted model of the same protein · chain A against A, TM-score 0.95

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q8N1Q8
Elsewhere: RCSB PDB 4AE7 · PDBe 4AE7 · UniProt Q8N1Q8

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