Research workbench
E. COLI gsp amidase C59 acetate modification
Analyse E. COLI gsp amidase C59 acetate modification in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3A30
- Type
- protein
- Length
- 179 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional glutathionylspermidine SYNTHETASE/AMIDASE
- EC
- 6.3.1.8, 3.5.1.78
- UniProt
- P0AES0
- Pockets
- 2 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional glutathionylspermidine SYNTHETASE/AMIDASE (EC 6.3.1.8, 3.5.1.78) | protein | 179 | 12% helix, 40% strand | P0AES0 |
Ligands and binding sites
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.39 | 0.81 | 14 | empty |
| 2 | 83 | 0.36 | 0.76 | 23 | ACT |
Modifications
Observed in the structure: 1 covalent (additive adduct).
Compared structures
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 P0AES0
- Elsewhere: RCSB PDB 3A30 · PDBe 3A30 · UniProt P0AES0
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