Research workbench
Crystal structure of glutamate complex of halotolerant γ-glutamyltranspeptidase from bacillus subtilis
Analyse Crystal structure of glutamate complex of halotolerant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3A75
- Type
- protein
- Length
- 1,083 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
- Ligands
- GLU
- Pockets
- 5 · best druggability 0.67
Structure
x-ray diffraction · 4 distinct chains · 38% 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 | 182 | 19% helix, 30% strand | P54422 |
| C | Gamma-glutamyltranspeptidase large chain (EC 2.3.2.2) | protein | 358 | 48% helix, 13% strand | P54422 |
| D | Gamma-glutamyltranspeptidase small chain (EC 2.3.2.2) | protein | 184 | 20% helix, 29% strand | P54422 |
Ligands and binding sites
- GLU · Glutamic acid · ligand · 2 copies · chains A, B, C, D
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 | 695 | 0.67 | 0.76 | 73 | GLU |
| 2 | 642 | 0.66 | 0.75 | 59 | GLU |
| 3 | 71 | 0.31 | 0.74 | 15 | empty |
| 4 | 51 | 0.29 | 0.75 | 20 | empty |
| 5 | 50 | 0.27 | 0.75 | 19 | empty |
Interfaces
3 interfaces between chains.
- C–D · 6667 Ų buried · 119 hydrogen bonds · protein-protein
- A–B · 6592 Ų buried · 110 hydrogen bonds · protein-protein
- A–C · 186 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 3A75 · Crystal structure of glutamate complex of halotolerant γ-glutamyltranspeptidase… · the same entry in another collection · chain C against C, TM-score 1.00
- P54422 · AlphaFold monomer V2.0 prediction for glutathione hydrolase proenzyme (P54422) · a predicted model of the same protein · chain C 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 3A75 · PDBe 3A75 · UniProt P54422
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