MolNFT v1 · #165492 · protein

Crystal structure of human FKBP51 FK1 domain A19T mutant in complex with hydantoin

6TX9 · Peptidyl-prolyl cis-trans isomerase FKBP5: “Crystal structure of human FKBP51 FK1 domain A19T mutant in complex with hydantoin”. X-ray diffraction, 2 ligands (HYN, NA), 1 pocket (best druggability 0.37). MolNFT v1 #165492 on…

PDB: 6TX9
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
Ligands: HYN, NA
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase FKBP5 (EC 5.2.1.8)	protein	128	16% helix, 38% strand	Q13451

Ligands and binding sites

HYN · imidazolidine-2,4-dione · ligand · chains A
NA · Sodium ion · metal · 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	63	0.37	0.78	15	HYN

Compared structures

6TX9 · Crystal structure of human FKBP51 FK1 domain A19T mutant in complex with hydantoin · 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 6TX9 · PDBe 6TX9 · UniProt Q13451

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