Research workbench
The von willebrand factor A3 domain binding region of type III collagen stabilized by the cysteine knot
Analyse The von willebrand factor A3 domain binding region of type III collagen… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GYX
- Type
- protein
- Length
- 82 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Type III collagen fragment in a host peptide stabilized by the cysteine knot
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Type III collagen fragment in a host peptide stabilized by the cysteine knot | protein | 28 | 0% helix, 0% strand | — |
| C | Type III collagen fragment in a host peptide stabilized by the cysteine knot | protein | 26 | 0% helix, 0% strand | — |
Interfaces
3 interfaces between chains.
- A–B · 936 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 861 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 853 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified, 1 disulfide (hydroxylation, disulfide).
Compared structures
- 4GYX · The von Willebrand Factor A3 domain binding region of type III collagen stabilized by the… · 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 4GYX · PDBe 4GYX
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