Research workbench
Structural and functional role of the imelysin-like protein efem from pseudomonas syringae pv. syringae and implications in bacterial iron transport
Analyse Structural and functional role of the imelysin-like protein efem from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BGO
- Type
- protein
- Length
- 502 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Efem M75 peptidase
- UniProt
- Q4ZR20
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 74% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Efem M75 peptidase | protein | 251 | 74% helix, 1% strand | Q4ZR20 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 7 copies · chains A, B
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 | 76 | 0.35 | 0.76 | 15 | empty |
| 2 | 65 | 0.30 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 703 Ų buried · 4 hydrogen bonds · protein-protein
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 Q4ZR20
- Elsewhere: RCSB PDB 4BGO · PDBe 4BGO · UniProt Q4ZR20
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