Research workbench
Crystal structure of (pro-pro-GLY)4-hyp-asp-gly-(pro-pro-GLY)4 at 1.02 a
Analyse Crystal structure of (pro-pro-GLY)4-hyp-asp-gly-(pro-pro-GLY)4 at 1.02 a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ABN
- Type
- protein
- Length
- 76 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagen-like peptide
Structure
x-ray diffraction · 3 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Collagen-like peptide | protein | 27 | 0% helix, 0% strand | — |
| B | Collagen-like peptide | protein | 25 | 0% helix, 0% strand | — |
| C | Collagen-like peptide | protein | 24 | 0% helix, 0% strand | — |
Interfaces
3 interfaces between chains.
- A–B · 749 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 720 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 719 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (hydroxylation).
Compared structures
- 3ABN · Crystal structure of (Pro-Pro-Gly)4-Hyp-Asp-Gly-(Pro-Pro-Gly)4 at 1.02 A · 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 3ABN · PDBe 3ABN
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