Research workbench
In-house sulfur-sad structure of orthorhombic red abalone lysin at 1.66 a resolution
Analyse In-house sulfur-sad structure of orthorhombic red abalone lysin at 1.66 a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5II7
- Type
- protein
- Length
- 132 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Egg-lysin
- UniProt
- P04552
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Egg-lysin | protein | 132 | 71% helix, 0% strand | P04552 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 9 copies · chains A
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5II7 · In-house sulfur-SAD structure of orthorhombic red abalone lysin at 1.66 A resolution · the same entry in another collection · chain A against A, TM-score 1.00
- P04552 · AlphaFold monomer V2.0 prediction for egg-lysin (P04552) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P04552
- Elsewhere: RCSB PDB 5II7 · PDBe 5II7 · UniProt P04552
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.