Research workbench
Structure of the visual signaling complex between transducin and phosphodiesterase 6
Analyse Structure of the visual signaling complex between transducin and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JSN
- Type
- protein
- Length
- 2,400 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rod cgmp-specific 3',5'-cyclic phosphodiesterase subunit alpha; Rod cgmp-specific…
- EC
- 3.1.4.35
- UniProt
- P11541, P23439, P04695, P04972
- Ligands
- VDN, 35G, GTP, ZN, MG
- Pockets
- 20 · best druggability 0.81
Structure
electron microscopy · 4 distinct chains · 46% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rod cgmp-specific 3',5'-cyclic phosphodiesterase subunit alpha (EC 3.1.4.35) | protein | 820 | 48% helix, 10% strand | P11541 |
| B | Rod cgmp-specific 3',5'-cyclic phosphodiesterase subunit beta (EC 3.1.4.35) | protein | 806 | 47% helix, 10% strand | P23439 |
| E, F | Guanine nucleotide-binding protein G(T) subunit alpha-1, guanine nucleotide-binding protein G(I) subunit alpha-1 chimera | protein | 316 | 45% helix, 14% strand | P04695 |
| C, D | Retinal rod rhodopsin-sensitive cgmp 3',5'-cyclic phosphodiesterase subunit gamma (EC 3.1.4.35) | protein | 71 | 13% helix, 3% strand | P04972 |
Ligands and binding sites
- VDN · 2-{2-ethoxy-5-[(4-ethylpiperazin-1-yl)sulfonyl]phenyl}-5-methyl-7-propylimidazo[5,1-f][1,2,4]triazin-4(1H)-one · ligand · 2 copies · chains A, B
- 35G · Guanosine-3',5'-monophosphate · ligand · 2 copies · chains A, B
- GTP · Guanosine-5'-triphosphate · ligand · 2 copies · chains E, F
- ZN · Zinc ion · metal · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1054 | 0.81 | 0.82 | 93 | empty |
| 2 | 692 | 0.80 | 0.84 | 65 | GTP |
| 3 | 185 | 0.79 | 0.94 | 27 | 35G |
| 4 | 712 | 0.78 | 0.82 | 76 | empty |
| 5 | 276 | 0.77 | 0.89 | 35 | 35G |
Interfaces
11 interfaces between chains.
- A–B · 5988 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 1616 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 1543 Ų buried · 7 hydrogen bonds · protein-protein
- F–D · 1270 Ų buried · 7 hydrogen bonds · protein-protein
- E–C · 1186 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 7JSN · Structure of the Visual Signaling Complex between Transducin and Phosphodiesterase 6 · the same entry in another collection · chain D against D, TM-score 1.00
- P04695 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(T) subunit… · a predicted model of the same protein · chain E against A, TM-score 0.96
- P23439 · AlphaFold monomer V2.0 prediction for rod cgmp-specific 3',5'-cyclic phosphodiesterase… · a predicted model of the same protein · chain B against A, TM-score 0.93
- P11541 · AlphaFold monomer V2.0 prediction for rod cgmp-specific 3',5'-cyclic phosphodiesterase… · a predicted model of the same protein · chain A against A, TM-score 0.92
- P04972 · AlphaFold monomer V2.0 prediction for retinal rod rhodopsin-sensitive cgmp 3',5'-cyclic… · a predicted model of the same protein · chain C against A, TM-score 0.26
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 P11541
- Every structure of UniProt P23439
- Every structure of UniProt P04695
- Every structure of UniProt P04972
- Elsewhere: RCSB PDB 7JSN · PDBe 7JSN · UniProt P11541 · UniProt P23439 · UniProt P04695 · UniProt P04972
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