MolNFT v1 · #165086 · protein
T. gondii myosin a trimeric complex with ELC1
6TJ5 · Calmodulin, putative: “T. gondii myosin a trimeric complex with ELC1”. X-ray diffraction, 2 ligands (CA, CL), 1 pocket (best druggability 0.39). MolNFT v1 #165086 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6TJ5
- Type
- protein
- Length
- 312 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin, putative; Myosin light chain TGMLC1; Myosin-a
- UniProt
- A0A0F7UZ05, Q95UJ7, O00934
- Ligands
- CA, CL
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 3 distinct chains · 63% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin, putative | protein | 131 | 60% helix, 8% strand | A0A0F7UZ05 |
| B | Myosin light chain TGMLC1 | protein | 137 | 59% helix, 9% strand | Q95UJ7 |
| C | Myosin-a | protein | 44 | 86% helix, 0% strand | O00934 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 109 | 0.39 | 0.75 | 17 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1359 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 1318 Ų buried · 24 hydrogen bonds · protein-protein
- A–B · 339 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
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 A0A0F7UZ05
- Every structure of UniProt Q95UJ7
- Every structure of UniProt O00934
- Elsewhere: RCSB PDB 6TJ5 · PDBe 6TJ5 · UniProt A0A0F7UZ05 · UniProt Q95UJ7 · UniProt O00934
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