Research workbench
Structural consequences of a discontinuity in the repeating tripeptide sequence of a collagen-like triple-helical peptide
Analyse Structural consequences of a discontinuity in the repeating tripeptide sequence… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EI8
- Type
- protein
- Length
- 171 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagen-like peptide (pro-hyp-GLY)4-pg-(pro-hyp- GLY)5
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D, E, F | Collagen-like peptide (pro-hyp-GLY)4-pg-(pro-hyp- GLY)5 | protein | 29 | 0% helix, 0% strand | — |
| C | Collagen-like peptide (pro-hyp-GLY)4-pg-(pro-hyp- GLY)5 | protein | 26 | 0% helix, 0% strand | — |
Interfaces
15 interfaces between chains.
- E–F · 909 Ų buried · 14 hydrogen bonds · protein-protein
- D–E · 901 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 900 Ų buried · 11 hydrogen bonds · protein-protein
- D–F · 851 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 832 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 53 modified (hydroxylation).
Compared structures
- 1EI8 · Structural consequences of a discontinuity in the repeating tripeptide sequence of a… · the same entry in another collection · chain D against D, 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 1EI8 · PDBe 1EI8
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