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Structure of the BTB/POZ domain of human 90K

Analyse Structure of the BTB/POZ domain of human 90K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6GFC
Type
protein
Length
722 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Galectin-3-binding protein
UniProt
H9FUB4
Pockets
4 · best druggability 0.68

Structure

x-ray diffraction · 5 distinct chains · 47% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CGalectin-3-binding proteinprotein11950% helix, 24% strandH9FUB4
BGalectin-3-binding proteinprotein12845% helix, 22% strandH9FUB4
DGalectin-3-binding proteinprotein12346% helix, 23% strandH9FUB4
FGalectin-3-binding proteinprotein10949% helix, 13% strandH9FUB4
GGalectin-3-binding proteinprotein12444% helix, 23% strandH9FUB4

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15260.680.7833empty
21380.450.7632empty
3930.390.7623empty
4690.300.7415empty

Interfaces

8 interfaces between chains.

  • A–B · 1536 Ų buried · 22 hydrogen bonds · protein-protein
  • F–G · 1513 Ų buried · 19 hydrogen bonds · protein-protein
  • C–D · 1468 Ų buried · 20 hydrogen bonds · protein-protein
  • A–D · 328 Ų buried · 1 hydrogen bond · protein-protein
  • B–C · 321 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

  • 6GFC · Structure of the BTB/POZ domain of human 90K · the same entry in another collection · chain A against A, TM-score 1.00

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