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Crystal structure of a transcription factor

Analyse Crystal structure of a transcription factor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7EQE
Type
protein
Length
706 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
TETR/ACRR family transcriptional regulator
UniProt
A0A4Z1DIH6
Pockets
9 · best druggability 0.80

Structure

x-ray diffraction · 4 distinct chains · 74% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATETR/ACRR family transcriptional regulatorprotein17970% helix, 0% strandA0A4Z1DIH6
BTETR/ACRR family transcriptional regulatorprotein17077% helix, 0% strandA0A4Z1DIH6
CTETR/ACRR family transcriptional regulatorprotein17973% helix, 0% strandA0A4Z1DIH6
DTETR/ACRR family transcriptional regulatorprotein17874% helix, 0% strandA0A4Z1DIH6

Pockets

9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110210.800.8182empty
211500.770.7997empty
31890.620.8321empty
41590.610.8421empty
51740.590.8221empty

Interfaces

4 interfaces between chains.

  • C–D · 1427 Ų buried · 14 hydrogen bonds · protein-protein
  • A–B · 1214 Ų buried · 11 hydrogen bonds · protein-protein
  • A–C · 394 Ų buried · 7 hydrogen bonds · protein-protein
  • B–C · 61 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

  • 7EQE · Crystal Structure of a transcription factor · the same entry in another collection · chain A against A, TM-score 1.00

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