MolNFT v1 · #73552 · protein

Crystal structure of a fragment of FKBP51 comprising the FK1 and FK2 domains

3O5D · Peptidyl-prolyl cis-trans isomerase FKBP5: “Crystal structure of a fragment of FKBP51 comprising the FK1 and FK2 domains”. X-ray diffraction, 5 pockets (best druggability 0.38). MolNFT v1 #73552 on GenesisL1: 3D structure, binding…

PDB: 3O5D
Type: protein
Length: 484 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: 5 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Peptidyl-prolyl cis-trans isomerase FKBP5 (EC 5.2.1.8)	protein	242	12% helix, 40% strand	Q13451

Pockets

5 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	66	0.38	0.78	14	empty
2	64	0.36	0.77	15	empty
3	57	0.32	0.77	16	empty
4	58	0.29	0.75	15	empty
5	69	0.29	0.73	18	empty

Interfaces

1 interface between chains.

A–B · 329 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

3O5D · Crystal structure of a fragment of FKBP51 comprising the Fk1 and Fk2 domains · 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 0.94

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 Q13451
Elsewhere: RCSB PDB 3O5D · PDBe 3O5D · UniProt Q13451

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