Research workbench

Homologous domain of human FKBP25

Analyse Homologous domain of human FKBP25 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PBK
Type: protein
Length: 116 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FKBP25
UniProt: Q00688
Ligands: RAP
Pockets: 1 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FKBP25	protein	116	11% helix, 36% strand	Q00688

Ligands and binding sites

RAP · Rapamycin immunosuppressant drug · ligand · 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	83	0.40	0.77	14	empty

Compared structures

1PBK · Homologous domain of human FKBP25 · the same entry in another collection · chain A against A, TM-score 1.00
Q00688 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP3 (Q00688) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q00688
Elsewhere: RCSB PDB 1PBK · PDBe 1PBK · UniProt Q00688

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