Research workbench
Crystal structure of gamma-glutamyl transferase from bacillus subtilis
Analyse Crystal structure of gamma-glutamyl transferase from bacillus subtilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2V36
- Type
- protein
- Length
- 1,074 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-glutamyltranspeptidase large chain; Gamma-glutamyltranspeptidase small chain
- EC
- 2.3.2.2
- UniProt
- P54422
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 4 distinct chains · 37% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gamma-glutamyltranspeptidase large chain (EC 2.3.2.2) | protein | 359 | 47% helix, 12% strand | P54422 |
| B | Gamma-glutamyltranspeptidase small chain (EC 2.3.2.2) | protein | 175 | 15% helix, 30% strand | P54422 |
| C | Gamma-glutamyltranspeptidase large chain (EC 2.3.2.2) | protein | 357 | 47% helix, 13% strand | P54422 |
| D | Gamma-glutamyltranspeptidase small chain (EC 2.3.2.2) | protein | 183 | 18% helix, 31% strand | P54422 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1067 | 0.72 | 0.76 | 104 | empty |
| 2 | 514 | 0.63 | 0.76 | 66 | empty |
| 3 | 55 | 0.29 | 0.75 | 19 | empty |
| 4 | 64 | 0.29 | 0.73 | 14 | empty |
Interfaces
3 interfaces between chains.
- C–D · 6575 Ų buried · 111 hydrogen bonds · protein-protein
- A–B · 6429 Ų buried · 109 hydrogen bonds · protein-protein
- A–D · 114 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2V36 · Crystal structure of gamma-glutamyl transferase from Bacillus subtilis · the same entry in another collection · chain D against D, TM-score 1.00
- P54422 · AlphaFold monomer V2.0 prediction for glutathione hydrolase proenzyme (P54422) · 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 P54422
- Elsewhere: RCSB PDB 2V36 · PDBe 2V36 · UniProt P54422
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