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NMR Study of the Fibrillin-1 cbEGF12-13 Pair of Ca2+ Binding Epidermal Growth Factor-like Domains
Analyse NMR Study of the Fibrillin-1 cbEGF12-13 Pair of Ca2+ Binding Epidermal Growth… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LMJ
- Type
- protein
- Length
- 86 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- NOT
- Source
- Homo sapiens
- Molecule
- fibrillin 1
- UniProt
- P35555
- Ligands
- CA
Structure
solution nmr · resolution NOT · 1 distinct chain · 5% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | fibrillin 1 | protein | 86 | 5% helix, 28% 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
- 1LMJ · NMR study of the fibrillin-1 CBEGF12-13 pair of CA2+ binding epidermal growth factor-like… · 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 1LMJ · PDBe 1LMJ · UniProt P35555
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