Research workbench
Structure of the cys-rich C-terminal domain of hydra minicollagen
Analyse Structure of the cys-rich C-terminal domain of hydra minicollagen in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SP7
- Type
- protein
- Length
- 24 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mini-collagen
- UniProt
- Q00484
Structure
solution nmr · 1 distinct chain · 21% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mini-collagen | protein | 24 | 21% helix, 0% strand | Q00484 |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1SP7 · Structure of the Cys-rich C-terminal domain of Hydra minicollagen · 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 Q00484
- Elsewhere: RCSB PDB 1SP7 · PDBe 1SP7 · UniProt Q00484
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