Research workbench
Structure of SACTELAM55A from streptomyces sp. sirexaa-E
Analyse Structure of SACTELAM55A from streptomyces sp. sirexaa-E in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PEW
- Type
- protein
- Length
- 1,097 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative secreted protein
- UniProt
- G2NFJ9
- Ligands
- MG
- Pockets
- 7 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative secreted protein | protein | 548 | 6% helix, 46% strand | G2NFJ9 |
| B | Putative secreted protein | protein | 549 | 6% helix, 45% strand | G2NFJ9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 78 | 0.76 | 0.99 | 29 | empty |
| 2 | 81 | 0.76 | 0.98 | 28 | empty |
| 3 | 617 | 0.69 | 0.78 | 63 | empty |
| 4 | 159 | 0.53 | 0.80 | 27 | MG |
| 5 | 157 | 0.53 | 0.80 | 21 | MG |
Interfaces
1 interface between chains.
- A–B · 447 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
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 G2NFJ9
- Elsewhere: RCSB PDB 4PEW · PDBe 4PEW · UniProt G2NFJ9
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.