Crystal structure of PDE6D in complex with compound 5e. Determined by X-ray diffraction at 1.65 Å resolution. Released 24 Dec 2025.
Explore 9HMC in 3D Show helices and sheets RCSB PDB PDBe
9HMC contains 7 α-helices and 18 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-13 | 10 | |
| β-strand | 15-24 | 10 | 1 |
| β-strand | 30-34 | 5 | 1 |
| β-strand | 44-49 | 6 | 2 |
| α-helix | 51-55 | 5 | |
| β-strand | 58-67 | 10 | 1 |
| β-strand | 71-82 | 12 | 2 |
| β-strand | 85-97 | 13 | 2 |
| β-strand | 101-110 | 10 | 1 |
| α-helix | 120-123 | 4 | |
| β-strand | 127-135 | 9 | 2 |
| β-strand | 138-149 | 12 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-13 | 12 | |
| β-strand | 15-24 | 10 | 3 |
| β-strand | 30-34 | 5 | 3 |
| β-strand | 44-49 | 6 | 4 |
| α-helix | 51-55 | 5 | |
| β-strand | 58-67 | 10 | 3 |
| β-strand | 71-82 | 12 | 4 |
| β-strand | 85-97 | 13 | 4 |
| β-strand | 101-110 | 10 | 3 |
| α-helix | 117-119 | 3 | |
| α-helix | 120-123 | 4 | |
| β-strand | 127-135 | 9 | 4 |
| β-strand | 138-149 | 12 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta | A, B | protein | 156 | Homo sapiens | O43924 (AlphaFold model) |
>9HMC_1 Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta (chains A, B) HHHHHHMSAKDERAREILRGFKLNWMNLRDAETGKILWQGTEDLSVPGVEHEARVPKKIL KCKAVSRELNFSSTEQMEKFRLEQKVYFKGQCLEEWFFEFGFVIPNSTNTWQSLIEAAPE SQMMPASVLTGNVIIETKFFDDDLLVSTSRVRLFYV
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1IWC | 4-[3,4-dimethyl-2-(4-methylphenyl)-7-oxidanylidene-pyrazolo[3,4-d]pyridazin-6-y… | C31 H48 N6 O3 S | 2 |
Water and common crystallization additives (PEG, GOL) are not listed.
Covalent modification of a glutamic acid inspired by HaloTag technology. Zhang, R., Liu, J., Gasper, R. et al. Nat Commun (2026) 17:1257-1257. DOI 10.1038/s41467-026-68999-9 · PubMed
Other PDB entries of the same protein (UniProt O43924 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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