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The 1.6 ångströms structure of the kunitz-type domain from the ALPHA3 chain of the human type VI collagen
Analyse The 1.6 ångströms structure of the kunitz-type domain from the ALPHA3 chain of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KNT
- Type
- protein
- Length
- 55 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagen type VI
- UniProt
- P12111
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Collagen type VI | protein | 55 | 22% helix, 31% strand | P12111 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1KNT · The 1.6 ångströms structure of the kunitz-type domain from the ALPHA3 chain of the human… · 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
- Every structure of UniProt P12111
- Elsewhere: RCSB PDB 1KNT · PDBe 1KNT · UniProt P12111
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