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Structure of apo P1 form of Candida albicans FKBP12

Analyse Structure of apo P1 form of Candida albicans FKBP12 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5HTG
Type
protein
Length
244 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.4
Source
Candida albicans (strain SC5314 / ATCC MYA-2876)
Molecule
FK506-binding protein 1
EC
5.2.1.8
UniProt
P28870
Pockets
5 · best druggability 0.49

Structure

x-ray diffraction · resolution 2.4 · 1 distinct chain · 15% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BFK506-binding protein 1 (EC 5.2.1.8)protein12215% helix, 36% strandP28870

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11610.490.7842empty
2610.360.7915empty
3740.350.7617empty
4570.330.7614empty
5530.310.7615empty

Interfaces

1 interface between chains.

  • A–B · 688 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 5HTG · Structure of apo P1 form of candida albicans FKBP12 · the same entry in another collection · chain A against A, TM-score 1.00
  • P28870 · AlphaFold monomer V2.0 prediction for FK506-binding protein 1 (P28870) · a predicted model of the same protein · chain A against A, TM-score 0.99

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