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Crystal structure of gamma-glutamyltranspeptidase from bacillus subtilis (crystal soaked for 0 min. in acivicin soln. )
Analyse Crystal structure of gamma-glutamyltranspeptidase 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
- 3WHQ
- Type
- protein
- Length
- 544 residues
- Chains
- 2
- 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, 3.4.19.13
- UniProt
- P54422
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gamma-glutamyltranspeptidase large chain (EC 2.3.2.2, 3.4.19.13) | protein | 360 | 48% helix, 12% strand | P54422 |
| B | Gamma-glutamyltranspeptidase small chain (EC 2.3.2.2, 3.4.19.13) | protein | 184 | 20% helix, 32% strand | P54422 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 809 | 0.70 | 0.77 | 69 | empty |
| 2 | 56 | 0.31 | 0.76 | 20 | empty |
| 3 | 53 | 0.25 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 6638 Ų buried · 112 hydrogen bonds · protein-protein
Compared structures
- 3WHQ · Crystal structure of gamma-glutamyltranspeptidase from Bacillus subtilis (crystal soaked… · the same entry in another collection · chain A against A, 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 3WHQ · PDBe 3WHQ · UniProt P54422
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