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Crystal structure of OSH1 ank domain from kluyveromyces lactis

Analyse Crystal structure of OSH1 ank domain from kluyveromyces lactis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5H2A
Type
protein
Length
528 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
KLLA0C04147P
UniProt
Q6CUK7
Pockets
2 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 58% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AKLLA0C04147Pprotein27159% helix, 0% strandQ6CUK7
BKLLA0C04147Pprotein25757% helix, 1% strandQ6CUK7

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11890.570.8028empty
2690.350.7615empty

Interfaces

1 interface between chains.

  • A–B · 702 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 5H2A · Crystal structure of Osh1 ANK domain from Kluyveromyces lactis · the same entry in another collection · chain A against A, TM-score 1.00

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