Research workbench
Structure of human soluble guanylate cyclase in the unliganded state
Analyse Structure of human soluble guanylate cyclase in the unliganded state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6JT0
- Type
- protein
- Length
- 1,118 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanylate cyclase soluble subunit alpha-1; Guanylate cyclase soluble subunit beta-1
- EC
- 4.6.1.2
- UniProt
- Q02108, Q02153
- Ligands
- HEM
- Pockets
- 15 · best druggability 0.83
Structure
electron microscopy · 2 distinct chains · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanylate cyclase soluble subunit alpha-1 (EC 4.6.1.2) | protein | 542 | 43% helix, 18% strand | Q02108 |
| B | Guanylate cyclase soluble subunit beta-1 (EC 4.6.1.2) | protein | 576 | 41% helix, 20% strand | Q02153 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 662 | 0.83 | 0.87 | 69 | HEM |
| 2 | 1049 | 0.81 | 0.83 | 100 | empty |
| 3 | 131 | 0.79 | 0.97 | 25 | empty |
| 4 | 477 | 0.77 | 0.85 | 42 | empty |
| 5 | 74 | 0.75 | 0.98 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 5333 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 6JT0 · Structure of human soluble guanylate cyclase in the unliganded state · the same entry in another collection · chain A against A, TM-score 1.00
- Q02108 · AlphaFold monomer V2.0 prediction for guanylate cyclase soluble subunit alpha-1 (Q02108) · a predicted model of the same protein · chain A against A, TM-score 0.54
- Q02153 · AlphaFold monomer V2.0 prediction for guanylate cyclase soluble subunit beta-1 (Q02153) · a predicted model of the same protein · chain B against A, TM-score 0.45
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 Q02108
- Every structure of UniProt Q02153
- Elsewhere: RCSB PDB 6JT0 · PDBe 6JT0 · UniProt Q02108 · UniProt Q02153
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