Research workbench
NMR study of a pair of fibrillin CA2+ binding epidermal growth factor- like domains, 22 structures
Analyse NMR study of a pair of fibrillin CA2+ binding epidermal growth factor- like… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EMO
- Type
- protein
- Length
- 82 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibrillin
- UniProt
- P35555
- Ligands
- CA
Structure
solution nmr · 1 distinct chain · 4% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibrillin | protein | 82 | 4% helix, 15% strand | P35555 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1EMO · NMR study of a pair of fibrillin CA2+ binding epidermal growth factor-like domains, 22… · 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 P35555
- Elsewhere: RCSB PDB 1EMO · PDBe 1EMO · UniProt P35555
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