Research workbench
Transglutaminase 2 undergoes large conformational change upon activation
Analyse Transglutaminase 2 undergoes large conformational change upon activation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q3Z
- Type
- protein
- Length
- 660 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transglutaminase 2; Polypeptide
- EC
- 2.3.2.13
- UniProt
- P21980
- Ligands
- ACE, SO4, NH2
- Pockets
- 7 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transglutaminase 2 (EC 2.3.2.13) | protein | 655 | 18% helix, 40% strand | P21980 |
| X | Polypeptide | protein | 5 | 0% helix, 20% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A, X
- SO4 · Sulfate ion · ion · 5 copies · chains A
- NH2 · Amino group · ion · chains A, X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 62 | 0.69 | 0.96 | 15 | empty |
| 2 | 420 | 0.66 | 0.79 | 46 | empty |
| 3 | 88 | 0.48 | 0.82 | 15 | empty |
| 4 | 97 | 0.41 | 0.77 | 24 | empty |
| 5 | 69 | 0.39 | 0.79 | 16 | empty |
Interfaces
1 interface between chains.
- A–X · 497 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent, 1 disulfide, 1 modified (covalent ligand, disulfide, nonstandard).
Compared structures
- 2Q3Z · Transglutaminase 2 undergoes large conformational change upon activation · the same entry in another collection · chain A against A, TM-score 1.00
- P21980 · AlphaFold monomer V2.0 prediction for protein-glutamine gamma- glutamyltransferase 2… · a predicted model of the same protein · chain A against A, TM-score 0.67
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P21980
- Elsewhere: RCSB PDB 2Q3Z · PDBe 2Q3Z · UniProt P21980
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