Research workbench
Crystal structure of acyl-CoA hydrolase from neisseria meningitidis FAM18
Analyse Crystal structure of acyl-CoA hydrolase from neisseria meningitidis FAM18 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IEN
- Type
- protein
- Length
- 616 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative acyl-CoA hydrolase
- EC
- 3.1.2.20
- UniProt
- A1KUS8
- Ligands
- COA, GDP, CL
- Pockets
- 9 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Putative acyl-CoA hydrolase (EC 3.1.2.20) | protein | 154 | 27% helix, 38% strand | A1KUS8 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 4 copies · chains A, B, C, D
- GDP · Guanosine-5'-diphosphate · ligand · 4 copies · chains A, B, C, D
- CL · Chloride ion · ion · 4 copies · chains A, B, C, 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, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 939 | 0.76 | 0.79 | 88 | GDP |
| 2 | 1170 | 0.76 | 0.78 | 115 | GDP |
| 3 | 136 | 0.60 | 0.84 | 26 | CL |
| 4 | 134 | 0.59 | 0.84 | 23 | CL |
| 5 | 162 | 0.59 | 0.82 | 24 | CL |
Interfaces
3 interfaces between chains.
- A–B · 1471 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 1466 Ų buried · 19 hydrogen bonds · protein-protein
- B–C · 602 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 4IEN · Crystal Structure of Acyl-CoA Hydrolase from Neisseria meningitidis FAM18 · 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 A1KUS8
- Elsewhere: RCSB PDB 4IEN · PDBe 4IEN · UniProt A1KUS8
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