MolNFT v1 · #3859 · protein
The role of phenylalanine 8 in the stabilization of the S protein-S peptide interaction: packing and cavities
1D5D: “The role of phenylalanine 8 in the stabilization of the S protein-S peptide interaction: packing and cavities”. X-ray diffraction, 1 ligand (SO4). MolNFT v1 #3859 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1D5D
- Type
- protein
- Length
- 116 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- S peptide; RNase S
- UniProt
- P61823, P00656
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains · 22% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S peptide | protein | 15 | 60% helix, 7% strand | P61823 |
| B | RNase S | protein | 101 | 17% helix, 43% strand | P00656 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 679 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide, 1 modified (disulfide, nonstandard).
Compared structures
- 1D5D · The role of phenylalanine 8 in the stabilization of the s protein-s peptide interaction… · 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 P61823
- Every structure of UniProt P00656
- Elsewhere: RCSB PDB 1D5D · PDBe 1D5D · UniProt P61823 · UniProt P00656
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