Research workbench
Crystal structure of ADENYLATE/GUANYLATE CYCLASE/HYDROLASE from silicibacter pomeroyi
Analyse Crystal structure of ADENYLATE/GUANYLATE CYCLASE/HYDROLASE from silicibacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MR7
- Type
- protein
- Length
- 514 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADENYLATE/GUANYLATE CYCLASE/HYDROLASE, ALPHA/BETA fold family
- UniProt
- Q5LP28
- Pockets
- 6 · best druggability 0.80
Structure
x-ray diffraction · 3 distinct chains · 37% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADENYLATE/GUANYLATE CYCLASE/HYDROLASE, ALPHA/BETA fold family | protein | 173 | 37% helix, 35% strand | Q5LP28 |
| B | ADENYLATE/GUANYLATE CYCLASE/HYDROLASE, ALPHA/BETA fold family | protein | 172 | 35% helix, 33% strand | Q5LP28 |
| C | ADENYLATE/GUANYLATE CYCLASE/HYDROLASE, ALPHA/BETA fold family | protein | 169 | 38% helix, 34% strand | Q5LP28 |
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1034 | 0.80 | 0.82 | 108 | empty |
| 2 | 102 | 0.71 | 0.93 | 25 | empty |
| 3 | 260 | 0.63 | 0.81 | 36 | empty |
| 4 | 173 | 0.55 | 0.79 | 29 | empty |
| 5 | 76 | 0.41 | 0.79 | 16 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1488 Ų buried · 22 hydrogen bonds · protein-protein
- A–C · 1080 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 3MR7 · Crystal Structure of Adenylate/Guanylate Cyclase/Hydrolase from Silicibacter pomeroyi · 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 Q5LP28
- Elsewhere: RCSB PDB 3MR7 · PDBe 3MR7 · UniProt Q5LP28
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