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Crystal structure of a linear-specific ubiquitin Fab bound to linear ubiquitin

Analyse Crystal structure of a linear-specific ubiquitin Fab bound to linear ubiquitin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3U30
Type
protein
Length
1,152 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Linear di-ubiquitin; Light chain Fab; Heavy chain Fab
UniProt
P0CG48
Pockets
13 · best druggability 0.60

Structure

x-ray diffraction · 4 distinct chains · 13% helix, 43% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALinear di-ubiquitinprotein14924% helix, 36% strandP0CG48
B, ELight chain Fabprotein2116% helix, 47% strand—
C, FHeavy chain Fabprotein2184% helix, 51% strand—
DLinear di-ubiquitinprotein14525% helix, 32% strandP0CG48

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14210.600.7644empty
24550.590.7547empty
34730.570.7354empty
41530.540.8025empty
5750.400.7921empty

Interfaces

8 interfaces between chains.

  • E–F · 1848 Ų buried · 15 hydrogen bonds · protein-protein
  • B–C · 1822 Ų buried · 12 hydrogen bonds · protein-protein
  • A–C · 832 Ų buried · 10 hydrogen bonds · protein-protein
  • D–F · 797 Ų buried · 7 hydrogen bonds · protein-protein
  • C–E · 414 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 3U30 · Crystal structure of a linear-specific Ubiquitin fab bound to linear ubiquitin · the same entry in another collection · chain E against E, TM-score 1.00

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