MolNFT v1 · #16289 · protein
Role of calcium ions in the activation and activity of the transglutaminase 3 enzyme
1NUF · Protein-glutamine glutamyltransferase E: “Role of calcium ions in the activation and activity of the transglutaminase 3 enzyme”. X-ray diffraction, 3 ligands (CA, CL, BR), 5 pockets (best druggability 0.67). MolNFT v1 #16289 on…
- PDB
- 1NUF
- Type
- protein
- Length
- 675 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein-glutamine glutamyltransferase E
- EC
- 2.3.2.13
- UniProt
- Q08188
- Ligands
- CA, CL, BR
- Pockets
- 5 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein-glutamine glutamyltransferase E (EC 2.3.2.13) | protein | 675 | 17% helix, 42% strand | Q08188 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
- CL · Chloride ion · ion · 4 copies · chains A
- BR · Bromide ion · ion · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 293 | 0.67 | 0.82 | 35 | empty |
| 2 | 312 | 0.64 | 0.80 | 34 | empty |
| 3 | 151 | 0.46 | 0.76 | 27 | empty |
| 4 | 117 | 0.38 | 0.75 | 25 | CL |
| 5 | 53 | 0.35 | 0.79 | 19 | CA |
Compared structures
- 1NUF · Role of Calcium Ions in the Activation and Activity of the Transglutaminase 3 Enzyme · the same entry in another collection · chain A against A, TM-score 1.00
- Q08188 · AlphaFold monomer V2.0 prediction for protein-glutamine gamma- glutamyltransferase E… · a predicted model of the same protein · chain A against A, TM-score 1.00
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 Q08188
- Elsewhere: RCSB PDB 1NUF · PDBe 1NUF · UniProt Q08188
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