Research workbench
Crystal structure of the signaling helix coiled-coil doimain of the beta-1 subunit of the soluble guanylyl cyclase
Analyse Crystal structure of the signaling helix coiled-coil doimain of the beta-1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HLS
- Type
- protein
- Length
- 506 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanylate cyclase soluble subunit beta-1
- EC
- 4.6.1.2
- UniProt
- P20595
- Pockets
- 3 · best druggability 0.49
Structure
x-ray diffraction · 5 distinct chains · 87% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanylate cyclase soluble subunit beta-1 (EC 4.6.1.2) | protein | 65 | 86% helix, 0% strand | P20595 |
| B | Guanylate cyclase soluble subunit beta-1 (EC 4.6.1.2) | protein | 63 | 89% helix, 0% strand | P20595 |
| C, D, G, H | Guanylate cyclase soluble subunit beta-1 (EC 4.6.1.2) | protein | 63 | 86% helix, 0% strand | P20595 |
| E | Guanylate cyclase soluble subunit beta-1 (EC 4.6.1.2) | protein | 64 | 86% helix, 3% strand | P20595 |
| F | Guanylate cyclase soluble subunit beta-1 (EC 4.6.1.2) | protein | 62 | 89% helix, 0% strand | P20595 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 133 | 0.49 | 0.79 | 20 | empty |
| 2 | 121 | 0.41 | 0.76 | 22 | empty |
| 3 | 54 | 0.33 | 0.77 | 16 | empty |
Interfaces
13 interfaces between chains.
- C–D · 1585 Ų buried · 14 hydrogen bonds · protein-protein
- G–H · 1570 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 1488 Ų buried · 16 hydrogen bonds · protein-protein
- E–F · 1471 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 1380 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 3HLS · Crystal structure of the signaling helix coiled-coil doimain of the BETA-1 subunit of the… · the same entry in another collection · chain H against H, TM-score 1.00
- P20595 · AlphaFold monomer V2.0 prediction for guanylate cyclase soluble subunit beta-1 (P20595) · a predicted model of the same protein · chain F against A, TM-score 0.66
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 P20595
- Elsewhere: RCSB PDB 3HLS · PDBe 3HLS · UniProt P20595
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