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Crystal structure of native fused 4-ot

Analyse Crystal structure of native fused 4-ot in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6BLM
Type
protein
Length
381 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
4-oxalocrotonate tautomerase
UniProt
Q392K7
Pockets
5 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C4-oxalocrotonate tautomeraseprotein12739% helix, 30% strandQ392K7

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1590.720.9727empty
22030.520.7733empty
31110.420.7718empty
4680.300.7418empty
5510.280.7517empty

Interfaces

3 interfaces between chains.

  • A–C · 1343 Ų buried · 20 hydrogen bonds · protein-protein
  • A–B · 1335 Ų buried · 25 hydrogen bonds · protein-protein
  • B–C · 1313 Ų buried · 15 hydrogen bonds · protein-protein

Compared structures

  • 6BLM · Crystal Structure of Native Fused 4-OT · the same entry in another collection · chain A against A, TM-score 1.00

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