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Crystal structure of btubc (bklc) from P. vanneervenii

Analyse Crystal structure of btubc (bklc) from P. vanneervenii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5O01
Type
protein
Length
508 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Bklc (bacterial kinesin-light chain-like)
UniProt
A8Y5U5
Pockets
3 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BBklc (bacterial kinesin-light chain-like)protein25476% helix, 0% strandA8Y5U5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15410.710.8050empty
21840.480.7622empty
3800.300.7221empty

Interfaces

1 interface between chains.

  • A–B · 745 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 5O01 · Crystal structure of BtubC (BKLC) from P. vanneervenii · the same entry in another collection · chain A against A, TM-score 1.00

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