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Crystal structure of N(1-260) of human FKBP52

Analyse Crystal structure of N(1-260) of human FKBP52 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Q1C
Type: protein
Length: 237 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FK506-binding protein 4
EC: 5.2.1.8
UniProt: Q02790
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FK506-binding protein 4 (EC 5.2.1.8)	protein	237	11% helix, 40% strand	Q02790

Ligands and binding sites

DMS · Dimethyl sulfoxide · additive · 5 copies · chains A
EDO · 1,2-ethanediol · additive · 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	52	0.35	0.78	11	DMS

Compared structures

1Q1C · Crystal structure of N(1-260) of human FKBP52 · the same entry in another collection · chain A against A, TM-score 1.00
Q02790 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP4 (Q02790) · 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 Q02790
Elsewhere: RCSB PDB 1Q1C · PDBe 1Q1C · UniProt Q02790

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