Research workbench
Valine-containing collagen peptide
Analyse Valine-containing collagen peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6W46
- Type
- protein
- Length
- 90 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagen-like peptide
- Ligands
- NH2
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Collagen-like peptide | protein | 30 | 0% helix, 0% strand | — |
Ligands and binding sites
- NH2 · Amino group · ion · 3 copies · chains A, B, C
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- B–C · 951 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 910 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 893 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 33 modified (hydroxylation, nonstandard).
Compared structures
- 6W46 · Valine-Containing Collagen Peptide · 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
- Elsewhere: RCSB PDB 6W46 · PDBe 6W46
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