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Structure of C. glabrata FKBP12-FK506 complex

Analyse Structure of C. glabrata FKBP12-FK506 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HUA
Type: protein
Length: 113 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FK506-binding protein 1
EC: 5.2.1.8
UniProt: Q6FMA3
Ligands: FK5
Pockets: 1 · best druggability 0.44

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FK506-binding protein 1 (EC 5.2.1.8)	protein	113	13% helix, 39% strand	Q6FMA3

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	97	0.44	0.78	13	empty

Compared structures

5HUA · Structure of C. glabrata FKBP12-FK506 complex · the same entry in another collection · chain A against A, TM-score 1.00
Q6FMA3 · AlphaFold monomer V2.0 prediction for FK506-binding protein 1 (Q6FMA3) · 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 Q6FMA3
Elsewhere: RCSB PDB 5HUA · PDBe 5HUA · UniProt Q6FMA3

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