Research workbench
Crystal structures of N-acyl homoserine lactonase aidh S102G mutant
Analyse Crystal structures of N-acyl homoserine lactonase aidh S102G mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4G8D
- Type
- protein
- Length
- 550 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ALPHA/BETA hydrolase fold protein
- UniProt
- D2J2T6
- Pockets
- 4 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ALPHA/BETA hydrolase fold protein | protein | 277 | 45% helix, 18% strand | D2J2T6 |
| B | ALPHA/BETA hydrolase fold protein | protein | 273 | 45% helix, 18% strand | D2J2T6 |
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 91 | 0.77 | 0.98 | 21 | empty |
| 2 | 157 | 0.74 | 0.91 | 29 | empty |
| 3 | 301 | 0.66 | 0.82 | 52 | empty |
| 4 | 211 | 0.57 | 0.80 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 999 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 4G8D · Crystal structures of N-acyl homoserine lactonase AidH S102G mutant · the same entry in another collection · 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 D2J2T6
- Elsewhere: RCSB PDB 4G8D · PDBe 4G8D · UniProt D2J2T6
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