Research workbench

FK1 domain of FKBP51, crystal form II

Analyse FK1 domain of FKBP51, crystal form II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3O5I
Type: protein
Length: 256 residues
Chains: 2
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
Pockets: 2 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Peptidyl-prolyl cis-trans isomerase FKBP5 (EC 5.2.1.8)	protein	128	14% helix, 36% strand	Q13451

Ligands and binding sites

GOL · Glycerol · additive · chains B
ACT · Acetate ion · additive · chains B

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	60	0.35	0.77	13	empty
2	52	0.34	0.78	14	empty

Compared structures

3O5I · Fk1 domain of FKBP51, crystal form II · 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 0.98

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 Q13451
Elsewhere: RCSB PDB 3O5I · PDBe 3O5I · UniProt Q13451

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