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Crystal structure of the 35-36 8 glycine insertion mutant of ubiquitin

Analyse Crystal structure of the 35-36 8 glycine insertion mutant of ubiquitin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2GBM
Type
protein
Length
321 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ubiquitin
UniProt
P62988
Ligands
ARS
Pockets
4 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 23% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUbiquitinprotein8121% helix, 31% strandP62988
B, C, DUbiquitinprotein8025% helix, 31% strandP62988

Ligands and binding sites

  • ARS · Arsenic · metal · 3 copies · chains B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14410.670.7949empty
2830.510.8320empty
3740.350.7620empty
4950.340.7416empty

Interfaces

4 interfaces between chains.

  • A–B · 363 Ų buried · 2 hydrogen bonds · protein-protein
  • B–C · 355 Ų buried · 13 hydrogen bonds · protein-protein
  • C–D · 257 Ų buried · 8 hydrogen bonds · protein-protein
  • B–D · 257 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 2GBM · Crystal Structure of the 35-36 8 Glycine Insertion Mutant of Ubiquitin · the same entry in another collection · chain A against A, TM-score 1.00

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