Research workbench
Structure of (PPG)4-opg-(PPG)4, monoclinic, twinned crystal
Analyse Structure of (PPG)4-opg-(PPG)4, monoclinic, twinned crystal in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3A0A
- Type
- protein
- Length
- 135 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagen-like peptide
Structure
x-ray diffraction · 5 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Collagen-like peptide | protein | 23 | 0% helix, 0% strand | — |
| B, E | Collagen-like peptide | protein | 22 | 0% helix, 0% strand | — |
| C | Collagen-like peptide | protein | 24 | 0% helix, 0% strand | — |
| D | Collagen-like peptide | protein | 22 | 0% helix, 0% strand | — |
| F | Collagen-like peptide | protein | 22 | 0% helix, 0% strand | — |
Interfaces
12 interfaces between chains.
- A–C · 698 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 663 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 663 Ų buried · 8 hydrogen bonds · protein-protein
- D–F · 652 Ų buried · 7 hydrogen bonds · protein-protein
- D–E · 635 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (hydroxylation).
Compared structures
- 3A0A · Structure of (PPG)4-OPG-(PPG)4, monoclinic, twinned crystal · 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 3A0A · PDBe 3A0A
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