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Crystal structure of the bric-a-brac (btb) domain of human BACH1

Analyse Crystal structure of the bric-a-brac (btb) domain of human BACH1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2IHC
Type
protein
Length
462 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transcription regulator protein BACH1
UniProt
O14867
Pockets
2 · best druggability 0.61

Structure

x-ray diffraction · 4 distinct chains · 49% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATranscription regulator protein BACH1protein11750% helix, 22% strandO14867
BTranscription regulator protein BACH1protein11347% helix, 23% strandO14867
CTranscription regulator protein BACH1protein11749% helix, 22% strandO14867
DTranscription regulator protein BACH1protein11551% helix, 22% strandO14867

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13530.610.7861empty
2590.350.7815empty

Interfaces

6 interfaces between chains.

  • A–B · 1719 Ų buried · 27 hydrogen bonds · protein-protein
  • C–D · 1716 Ų buried · 24 hydrogen bonds · protein-protein
  • B–C · 407 Ų buried · 4 hydrogen bonds · protein-protein
  • B–D · 208 Ų buried · 3 hydrogen bonds · protein-protein
  • A–C · 193 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 2IHC · Crystal structure of the bric-a-brac (BTB) domain of human BACH1 · the same entry in another collection · chain D against D, TM-score 1.00
  • O14867 · AlphaFold monomer V2.0 prediction for transcription regulator protein BACH1 (O14867) · a predicted model of the same protein · chain B against A, TM-score 0.98

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