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Crystal structure of gamma-glutamyltranspeptidase from escherichia COLI (monoclinic form)
Analyse Crystal structure of gamma-glutamyltranspeptidase from escherichia COLI… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2E0X
- Type
- protein
- Length
- 1,076 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-glutamyltranspeptidase
- EC
- 2.3.2.2
- UniProt
- P18956
- Ligands
- CA
- Pockets
- 9 · best druggability 0.76
Structure
x-ray diffraction · 3 distinct chains · 34% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Gamma-glutamyltranspeptidase (EC 2.3.2.2) | protein | 359 | 46% helix, 13% strand | P18956 |
| B | Gamma-glutamyltranspeptidase (EC 2.3.2.2) | protein | 178 | 20% helix, 29% strand | P18956 |
| D | Gamma-glutamyltranspeptidase (EC 2.3.2.2) | protein | 180 | 22% helix, 28% strand | P18956 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 455 | 0.76 | 0.85 | 36 | CA |
| 2 | 520 | 0.75 | 0.83 | 55 | empty |
| 3 | 319 | 0.71 | 0.84 | 37 | empty |
| 4 | 297 | 0.71 | 0.85 | 37 | empty |
| 5 | 55 | 0.39 | 0.81 | 21 | empty |
Interfaces
6 interfaces between chains.
- C–D · 6495 Ų buried · 124 hydrogen bonds · protein-protein
- A–B · 6491 Ų buried · 123 hydrogen bonds · protein-protein
- B–C · 477 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 453 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 300 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 32 modified (engineered).
Compared structures
- 2E0X · Crystal Structure of Gamma-glutamyltranspeptidase from Escherichia coli (monoclinic form) · the same entry in another collection · chain D against D, TM-score 1.00
- P18956 · AlphaFold monomer V2.0 prediction for glutathione hydrolase proenzyme (P18956) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 P18956
- Elsewhere: RCSB PDB 2E0X · PDBe 2E0X · UniProt P18956
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