MolNFT v1 · #6696 · protein

Atomic structure of FKBP12-rapaymycin, an immunophilin- immunosuppressant complex

1FKL · FK506 binding protein: “Atomic structure of FKBP12-rapaymycin, an immunophilin- immunosuppressant complex”. X-ray diffraction, 1 ligand (RAP), 1 pocket (best druggability 0.43). MolNFT v1 #6696 on GenesisL1: 3D structure, binding…

PDB: 1FKL
Type: protein
Length: 107 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FK506 binding protein
EC: 5.2.1.8
UniProt: P18203
Ligands: RAP
Pockets: 1 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FK506 binding protein (EC 5.2.1.8)	protein	107	13% helix, 40% strand	P18203

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	95	0.43	0.77	13	empty

Compared structures

1FKL · Atomic structure of FKBP12-rapaymycin, an immunophilin-immunosuppressant complex · the same entry in another collection · chain A against A, TM-score 1.00
P18203 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP1A (P18203) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P18203
Elsewhere: RCSB PDB 1FKL · PDBe 1FKL · UniProt P18203

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