Research workbench
Crystal structure of the heterodimeric catalytic domain of wild-type human soluble guanylate cyclase
Analyse Crystal structure of the heterodimeric catalytic domain of wild-type human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NI2
- Type
- protein
- Length
- 390 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanylate cyclase soluble subunit alpha-3; Guanylate cyclase soluble subunit beta-1
- EC
- 4.6.1.2
- UniProt
- Q02108, Q02153
- Pockets
- 4 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanylate cyclase soluble subunit alpha-3 (EC 4.6.1.2) | protein | 192 | 32% helix, 31% strand | Q02108 |
| B | Guanylate cyclase soluble subunit beta-1 (EC 4.6.1.2) | protein | 198 | 30% helix, 34% strand | Q02153 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 496 | 0.74 | 0.82 | 42 | EDO |
| 2 | 548 | 0.70 | 0.79 | 60 | EDO |
| 3 | 80 | 0.48 | 0.83 | 20 | EDO |
| 4 | 70 | 0.36 | 0.77 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1417 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 4NI2 · Crystal structure of the heterodimeric catalytic domain of wild-type human soluble… · the same entry in another collection · chain A against A, TM-score 1.00
- 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 0.96
- 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 0.95
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 4NI2 · PDBe 4NI2 · UniProt Q02108 · UniProt Q02153
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.