Research workbench
Collagen model peptide (pro-pro-GLY)9
Analyse Collagen model peptide (pro-pro-GLY)9 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CUO
- Type
- protein
- Length
- 158 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagen model peptide (pro-pro-GLY)9
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D, E | Collagen model peptide (pro-pro-GLY)9 | protein | 26 | 0% helix, 0% strand | — |
| C, F | Collagen model peptide (pro-pro-GLY)9 | protein | 27 | 0% helix, 0% strand | — |
Interfaces
12 interfaces between chains.
- A–C · 765 Ų buried · 10 hydrogen bonds · protein-protein
- D–F · 763 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 760 Ų buried · 8 hydrogen bonds · protein-protein
- D–E · 758 Ų buried · 8 hydrogen bonds · protein-protein
- E–F · 753 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 2CUO · Collagen model peptide (PRO-PRO-GLY)9 · 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 2CUO · PDBe 2CUO
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.