Research workbench
Solution structures of the FN3 domain of human collagen alpha-1(XX) chain
Analyse Solution structures of the FN3 domain of human collagen alpha-1(XX) chain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EKJ
- Type
- protein
- Length
- 105 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagen alpha-1(XX) chain
- UniProt
- Q9P218
Structure
solution nmr · 1 distinct chain · 0% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Collagen alpha-1(XX) chain | protein | 105 | 0% helix, 32% strand | Q9P218 |
Compared structures
- 2EKJ · Solution structures of the fn3 domain of human collagen alpha-1(XX) chain · the same entry in another collection · chain A against A, TM-score 1.00
- Q9P218 · AlphaFold monomer V2.0 prediction for collagen alpha-1(XX) chain (Q9P218) · a predicted model of the same protein · chain A against A, TM-score 0.89
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 Q9P218
- Elsewhere: RCSB PDB 2EKJ · PDBe 2EKJ · UniProt Q9P218
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