Research workbench
Crystal structure of the tig domain of human calmodulin- binding transcription activator 1 (CAMTA1)
Analyse Crystal structure of the tig domain of human calmodulin- binding transcription… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CXK
- Type
- protein
- Length
- 427 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin binding transcription activator 1
- UniProt
- Q5VUE1
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.81
Structure
x-ray diffraction · 4 distinct chains · 0% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin binding transcription activator 1 | protein | 87 | 0% helix, 51% strand | Q5VUE1 |
| B, C | Calmodulin binding transcription activator 1 | protein | 85 | 0% helix, 52% strand | Q5VUE1 |
| D | Calmodulin binding transcription activator 1 | protein | 84 | 0% helix, 54% strand | Q5VUE1 |
| E | Calmodulin binding transcription activator 1 | protein | 86 | 0% helix, 55% strand | Q5VUE1 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 6 copies · chains A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1143 | 0.81 | 0.82 | 126 | SO4 |
| 2 | 106 | 0.45 | 0.78 | 22 | empty |
| 3 | 81 | 0.39 | 0.78 | 15 | empty |
Interfaces
8 interfaces between chains.
- A–B · 675 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 654 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 394 Ų buried · 3 hydrogen bonds · protein-protein
- D–E · 371 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 311 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
- 2CXK · Crystal structure of the TIG domain of human calmodulin-binding transcription activator 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 Q5VUE1
- Elsewhere: RCSB PDB 2CXK · PDBe 2CXK · UniProt Q5VUE1
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