Research workbench
The anisotropic refinement of kunitz type domain C5 at 0.95 ångström
Analyse The anisotropic refinement of kunitz type domain C5 at 0.95 ångström in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KTH
- Type
- protein
- Length
- 58 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagen alpha 3(VI) chain
- UniProt
- P12111
- Ligands
- PO4
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Collagen alpha 3(VI) chain | protein | 58 | 21% helix, 29% strand | P12111 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · 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
- 1KTH · The Anisotropic Refinement Of Kunitz Type Domain C5 at 0.95 Angstrom · 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 1KTH · PDBe 1KTH · UniProt P12111
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