Research workbench
Endolysin from escherichia COLI O157:H7 phage FAHEC1
Analyse Endolysin from escherichia COLI O157:H7 phage FAHEC1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7M5I
- Type
- protein
- Length
- 318 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0F6R9G3
- Ligands
- PO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 158 | — | A0A0F6R9G3 |
| A | — | protein | 160 | — | A0A0F6R9G3 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 4 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7M5I · Endolysin from Escherichia coli O157:H7 phage FAHEc1 · the same entry in another collection · chain B against B, 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 A0A0F6R9G3
- Elsewhere: RCSB PDB 7M5I · PDBe 7M5I · UniProt A0A0F6R9G3
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