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Structure of sting-associated cdne C-di-gmp synthase from capnocytophaga granulosa
Analyse Structure of sting-associated cdne C-di-gmp synthase from capnocytophaga… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WT9
- Type
- protein
- Length
- 301 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NTP_TRANSF_2 domain-containing protein
- UniProt
- A0A381HBN1
- Pockets
- 2 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NTP_TRANSF_2 domain-containing protein | protein | 301 | 53% helix, 15% strand | A0A381HBN1 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 345 | 0.60 | 0.77 | 37 | empty |
| 2 | 80 | 0.47 | 0.82 | 22 | empty |
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
- 6WT9 · Structure of STING-associated CdnE c-di-GMP synthase from Capnocytophaga granulosa · 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 A0A381HBN1
- Elsewhere: RCSB PDB 6WT9 · PDBe 6WT9 · UniProt A0A381HBN1
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