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Anomalous substructure of titin-A168169
Analyse Anomalous substructure of titin-A168169 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ILL
- Type
- protein
- Length
- 195 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Titin
- EC
- 2.7.11.1
- UniProt
- Q8WZ42
- Ligands
- CL
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Titin (EC 2.7.11.1) | protein | 195 | 3% helix, 59% strand | Q8WZ42 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2ILL · Anomalous substructure of Titin-A168169 · 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 Q8WZ42
- Elsewhere: RCSB PDB 2ILL · PDBe 2ILL · UniProt Q8WZ42
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