Research workbench
HSNMT1 in complex with CoA and myristoylated-gcsvskkk octapeptide
Analyse HSNMT1 in complex with CoA and myristoylated-gcsvskkk octapeptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5O9U
- Type
- protein
- Length
- 802 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P30419, O81223
- Ligands
- COA, MYR
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 393 | — | P30419 |
| C, D | — | protein | 8 | — | O81223 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 2 copies · chains A, C, B, D
- MYR · Myristic acid · ligand · 2 copies · chains A, C, B, D
- GOL · Glycerol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- P30419 · AlphaFold monomer V2.0 prediction for glycylpeptide N-tetradecanoyltransferase 1 (P30419) · a predicted model of the same protein · chain A against A, TM-score 1.00
- O81223 · AlphaFold monomer V2.0 prediction for calcineurin B-like protein 4 (O81223) · a predicted model of the same protein · chain C against A, TM-score 0.43
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 P30419
- Every structure of UniProt O81223
- Elsewhere: RCSB PDB 5O9U · PDBe 5O9U · UniProt P30419 · UniProt O81223
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