Research workbench
Structure of the tropomyosin overlap complex from chicken smooth muscle
Analyse Structure of the tropomyosin overlap complex from chicken smooth muscle in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MTU
- Type
- protein
- Length
- 410 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tropomyosin alpha-1 CHAIN,MICROTUBULE-associated protein RP/EB family member 1; Capsid…
- UniProt
- P04268, Q15691, P13848
- Ligands
- CL
- Pockets
- 3 · best druggability 0.50
Structure
x-ray diffraction · 5 distinct chains · 87% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tropomyosin alpha-1 CHAIN,MICROTUBULE-associated protein RP/EB family member 1 | protein | 75 | 81% helix, 3% strand | P04268, Q15691 |
| B | Tropomyosin alpha-1 CHAIN,MICROTUBULE-associated protein RP/EB family member 1 | protein | 68 | 88% helix, 0% strand | P04268, Q15691 |
| C | Tropomyosin alpha-1 CHAIN,MICROTUBULE-associated protein RP/EB family member 1 | protein | 66 | 88% helix, 0% strand | P04268, Q15691 |
| D | Tropomyosin alpha-1 CHAIN,MICROTUBULE-associated protein RP/EB family member 1 | protein | 67 | 87% helix, 0% strand | P04268, Q15691 |
| E, F | Capsid assembly scaffolding PROTEIN,TROPOMYOSIN alpha-1 chain | protein | 67 | 90% helix, 0% strand | P04268, P13848 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, C, D, B, F
- EDO · 1,2-ethanediol · additive · 9 copies · chains A, E, B, C, D, F
- EOH · Ethanol · additive · 7 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 97 | 0.50 | 0.81 | 13 | EDO |
| 2 | 72 | 0.42 | 0.80 | 13 | empty |
| 3 | 64 | 0.32 | 0.75 | 13 | empty |
Interfaces
13 interfaces between chains.
- C–D · 1915 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 1804 Ų buried · 15 hydrogen bonds · protein-protein
- E–F · 1624 Ų buried · 20 hydrogen bonds · protein-protein
- A–C · 639 Ų buried · 13 hydrogen bonds · protein-protein
- B–D · 442 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified (engineered).
Compared structures
- 3MTU · Structure of the Tropomyosin Overlap Complex from Chicken Smooth Muscle · the same entry in another collection · chain A against A, TM-score 1.00
- Q15691 · AlphaFold monomer V2.0 prediction for microtubule-associated protein RP/EB family member… · a predicted model of the same protein · chain D against A, TM-score 0.89
- P04268 · AlphaFold monomer V2.0 prediction for tropomyosin alpha-1 chain (P04268) · a predicted model of the same protein · chain E against A, TM-score 0.72
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 P04268
- Every structure of UniProt Q15691
- Every structure of UniProt P13848
- Elsewhere: RCSB PDB 3MTU · PDBe 3MTU · UniProt P04268 · UniProt Q15691 · UniProt P13848
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