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Human FKBP5 protein

Analyse Human FKBP5 protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5OMP
Type: protein
Length: 412 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase FKBP5
EC: 5.2.1.8
UniProt: Q13451
Ligands: SO4
Pockets: 3 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase FKBP5 (EC 5.2.1.8)	protein	412	42% helix, 24% strand	Q13451

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A

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

Pockets

3 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	259	0.50	0.74	37	empty
2	101	0.40	0.76	18	empty
3	58	0.36	0.78	13	empty

Compared structures

5OMP · Human FKBP5 protein · the same entry in another collection · chain A against A, TM-score 1.00
Q13451 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP5 (Q13451) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q13451
Elsewhere: RCSB PDB 5OMP · PDBe 5OMP · UniProt Q13451

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