Research workbench
Structure of CTATM1 in the inward-open with glutathione-complexed [2FE-2S] cluster bound
Analyse Structure of CTATM1 in the inward-open with glutathione-complexed [2FE-2S]… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PRO
- Type
- protein
- Length
- 1,160 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative iron-sulfur protein
- UniProt
- G0SBE6
- Pockets
- 12 · best druggability 0.79
Structure
electron microscopy · 1 distinct chain · 61% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Putative iron-sulfur protein | protein | 580 | 61% helix, 9% strand | G0SBE6 |
Pockets
12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1138 | 0.79 | 0.81 | 95 | empty |
| 2 | 61 | 0.60 | 0.91 | 18 | empty |
| 3 | 63 | 0.59 | 0.90 | 17 | empty |
| 4 | 169 | 0.48 | 0.76 | 29 | empty |
| 5 | 137 | 0.47 | 0.78 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 5744 Ų buried · 27 hydrogen bonds · protein-protein
Compared structures
- 7PRO · Structure of CtAtm1 in the inward-open with Glutathione-complexed [2Fe-2S] cluster bound · 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 G0SBE6
- Elsewhere: RCSB PDB 7PRO · PDBe 7PRO · UniProt G0SBE6
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