Research workbench
Structure of a covalently captured collagen triple helix using lysine- glutamate pairs
Analyse Structure of a covalently captured collagen triple helix using lysine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VZX
- Type
- protein
- Length
- 72 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagen mimetic peptide
- Ligands
- ACE, NH2
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Collagen mimetic peptide | protein | 24 | 0% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 3 copies · chains A, B, C
- NH2 · Amino group · ion · 3 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.
- A–C · 750 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 748 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 722 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 21 modified, 3 covalent, 3 isopeptide (hydroxylation, covalent ligand, isopeptide).
Compared structures
- 6VZX · Structure of a Covalently Captured Collagen Triple Helix using Lysine-Glutamate Pairs · 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 6VZX · PDBe 6VZX
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