Research workbench
The crystal structure of acyl-CoA synthetase (AMP-FORMING)/AMP-acid ligase II-like protein from dyadobacter fermentans dsm 18053
Analyse The crystal structure of acyl-CoA synthetase (AMP-FORMING)/AMP-acid ligase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GS5
- Type
- protein
- Length
- 350 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acyl-CoA synthetase (AMP-FORMING)/AMP-acid ligase II-like protein
- UniProt
- C6W5A4
- Ligands
- IOD
- Pockets
- 2 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acyl-CoA synthetase (AMP-FORMING)/AMP-acid ligase II-like protein | protein | 350 | 33% helix, 30% strand | C6W5A4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 239 | 0.56 | 0.78 | 29 | IOD, EDO |
| 2 | 56 | 0.27 | 0.74 | 18 | IOD |
Modifications
Observed in the structure: 13 modified (engineered).
Compared structures
- 4GS5 · The crystal structure of acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II-like… · 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 C6W5A4
- Elsewhere: RCSB PDB 4GS5 · PDBe 4GS5 · UniProt C6W5A4
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