Research workbench

Crystal structure of the FK506-binding domain of human FKBP38

Analyse Crystal structure of the FK506-binding domain of human FKBP38 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3EY6
Type: protein
Length: 118 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FK506-binding protein 8
EC: 5.2.1.8
UniProt: Q14318
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FK506-binding protein 8 (EC 5.2.1.8)	protein	118	11% helix, 42% strand	Q14318

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	64	0.36	0.77	14	empty

Compared structures

3EY6 · Crystal structure of the FK506-binding domain of human FKBP38 · the same entry in another collection · chain A against A, TM-score 1.00
Q14318 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP8 (Q14318) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q14318
Elsewhere: RCSB PDB 3EY6 · PDBe 3EY6 · UniProt Q14318

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.