MolNFT v1 · #28325 · protein

Improved calcineurin inhibition by yeast FKBP12-drug complexes. crystallographic and functional analysis

1YAT · FK506 binding protein: “Improved calcineurin inhibition by yeast FKBP12-drug complexes. crystallographic and functional analysis”. X-ray diffraction, 1 ligand (FK5), 1 pocket (best druggability 0.43). MolNFT v1 #28325 on GenesisL1…

PDB: 1YAT
Type: protein
Length: 113 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FK506 binding protein
UniProt: P20081
Ligands: FK5
Pockets: 1 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FK506 binding protein	protein	113	13% helix, 39% strand	P20081

Ligands and binding sites

FK5 · 8-deethyl-8-[but-3-enyl]-ascomycin · 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	89	0.43	0.77	13	empty

Compared structures

1YAT · Improved calcineurin inhibition by yeast FKBP12-drug complexes. crystallographic and… · the same entry in another collection · chain A against A, TM-score 1.00
P20081 · AlphaFold monomer V2.0 prediction for FK506-binding protein 1 (P20081) · 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 P20081
Elsewhere: RCSB PDB 1YAT · PDBe 1YAT · UniProt P20081

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