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FK1 domain mutant A19T of FKBP51, crystal form IV, in presence of dmso

Analyse FK1 domain mutant A19T of FKBP51, crystal form IV, in presence of dmso in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3O5Q
Type: protein
Length: 128 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
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase FKBP5 (EC 5.2.1.8)	protein	128	17% helix, 36% strand	Q13451

Ligands and binding sites

DMS · Dimethyl sulfoxide · additive · 2 copies · chains A

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

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	56	0.37	0.79	13	DMS

Compared structures

3O5Q · Fk1 domain mutant A19T of FKBP51, crystal form IV, in presence of DMSO · 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 3O5Q · PDBe 3O5Q · UniProt Q13451

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