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TAB2 nzf domain in complex with LYS63-linked di-ubiquitin, P212121

Analyse TAB2 nzf domain in complex with LYS63-linked di-ubiquitin, P212121 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2WWZ
Type
protein
Length
180 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ubiquitin; Mitogen-activated protein kinase kinase kinase 7- interacting protein 2
UniProt
P62990, Q9NYJ8
Ligands
ZN
Pockets
2 · best druggability 0.61

Structure

x-ray diffraction · 3 distinct chains · 20% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUbiquitinprotein7624% helix, 34% strandP62990
BUbiquitinprotein7225% helix, 36% strandP62990
CMitogen-activated protein kinase kinase kinase 7- interacting protein 2protein320% helix, 19% strandQ9NYJ8

Ligands and binding sites

  • ZN · Zinc ion · metal · chains C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12830.610.8034empty
2630.450.8317empty

Interfaces

3 interfaces between chains.

  • B–C · 424 Ų buried · 6 hydrogen bonds · protein-protein
  • A–C · 410 Ų buried · 5 hydrogen bonds · protein-protein
  • A–B · 167 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 isopeptide (isopeptide).

Compared structures

  • 2WWZ · TAB2 NZF DOMAIN IN COMPLEX WITH Lys63-linked di-ubiquitin, P212121 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9NYJ8 · AlphaFold monomer V2.0 prediction for TGF-beta-activated kinase 1 and MAP3K7-binding… · a predicted model of the same protein · chain C against A, TM-score 0.83

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