Research workbench
Saposin-like protein ac-slp-1
Analyse Saposin-like protein ac-slp-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3S64
- Type
- protein
- Length
- 81 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Saposin-like protein 1
- UniProt
- Q0MRQ4
Structure
x-ray diffraction · 1 distinct chain · 64% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Saposin-like protein 1 | protein | 81 | 64% helix, 0% strand | Q0MRQ4 |
Ligands and binding sites
- CIT · Citric acid · additive · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 3S64 · Saposin-like protein Ac-SLP-1 · 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 Q0MRQ4
- Elsewhere: RCSB PDB 3S64 · PDBe 3S64 · UniProt Q0MRQ4
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