Research workbench
The laminin-binding domain of agrin is structurally related to N-timp-1
Analyse The laminin-binding domain of agrin is structurally related to N-timp-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JC7
- Type
- protein
- Length
- 129 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Agrin
- UniProt
- Q90685
- Ligands
- CL
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Agrin | protein | 129 | 23% helix, 40% strand | Q90685 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1JC7 · The Laminin-Binding Domain of Agrin is Structurally Related to N-TIMP-1 · 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 Q90685
- Elsewhere: RCSB PDB 1JC7 · PDBe 1JC7 · UniProt Q90685
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