Research workbench
Cytoplasmic domain of the thermomonospora curvata type VII secretion ATPase eccc
Analyse Cytoplasmic domain of the thermomonospora curvata type VII secretion ATPase eccc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NH0
- Type
- protein
- Length
- 1,720 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell DIVISIONFTSK/SPOIIIE
- UniProt
- D1A4G7
- Ligands
- ATP, MG, SO4
- Pockets
- 20 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell DIVISIONFTSK/SPOIIIE | protein | 861 | 33% helix, 22% strand | D1A4G7 |
| B | Cell DIVISIONFTSK/SPOIIIE | protein | 859 | 33% helix, 20% strand | D1A4G7 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 4 copies · chains A, B
- MG · Magnesium ion · metal · 4 copies · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 295 | 0.69 | 0.83 | 30 | empty |
| 2 | 463 | 0.69 | 0.80 | 56 | MG, ATP |
| 3 | 284 | 0.68 | 0.83 | 30 | empty |
| 4 | 230 | 0.58 | 0.79 | 23 | empty |
| 5 | 119 | 0.47 | 0.79 | 25 | empty |
Compared structures
- 4NH0 · Cytoplasmic domain of the Thermomonospora curvata Type VII Secretion ATPase EccC · the same entry in another collection · chain A against A, TM-score 1.00
- D1A4G7 · AlphaFold monomer V2.0 prediction for esx secretion system protein eccc (D1A4G7) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 D1A4G7
- Elsewhere: RCSB PDB 4NH0 · PDBe 4NH0 · UniProt D1A4G7
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