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Crystal structure of USP7 catalytic domain [V302K] mutant in complex with ubiquitin

Analyse Crystal structure of USP7 catalytic domain [V302K] mutant in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5KYD
Type
protein
Length
417 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Polyubiquitin-B; Ubiquitin carboxyl-terminal hydrolase 7
EC
3.4.19.12
UniProt
P0CG47, Q93009
Pockets
5 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
DPolyubiquitin-Bprotein7625% helix, 33% strandP0CG47
AUbiquitin carboxyl-terminal hydrolase 7 (EC 3.4.19.12)protein34132% helix, 28% strandQ93009

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14680.800.8863empty
21210.410.7520empty
3590.340.7714empty
4770.320.7422empty
5630.300.7416empty

Interfaces

1 interface between chains.

  • D–A · 1491 Ų buried · 31 hydrogen bonds · protein-protein

Compared structures

  • 5KYD · Crystal structure of USP7 catalytic domain [V302K] mutant in complex with ubiquitin · the same entry in another collection · chain D against D, TM-score 1.00

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