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The E. COLI biotin holoenzyme SYNTHETASE(SLASH)BIO repressor crystal structure delineates the biotin and DNA- binding domains

Analyse The E. COLI biotin holoenzyme SYNTHETASE(SLASH)BIO repressor crystal structure… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1BIA
Type
protein
Length
292 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Bira bifunctional protein
EC
6.3.4.15
UniProt
P06709
Pockets
2 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABira bifunctional protein (EC 6.3.4.15)protein29233% helix, 29% strandP06709

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11860.570.8025empty
2680.290.7420empty

Compared structures

  • 1BIA · The E. COLI biotin holoenzyme SYNTHETASE(SLASH)BIO repressor crystal structure delineates… · the same entry in another collection · chain A against A, TM-score 1.00
  • P06709 · AlphaFold monomer V2.0 prediction for bifunctional LIGASE/REPRESSOR bira (P06709) · a predicted model of the same protein · chain A against A, TM-score 0.95

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