Download MendeleyHuman NAT16 encodes histidine alpha-acetyltransferase
Myllykoski, M., Osberg, C., Lundekvam, M., Arnesen, T.To be published.
9EMP | pdb_00009emp
Crystal structure of Histidine acetyltransferase with N-myristoyl histidine and coenzyme A
- PDB DOI: https://doi.org/10.2210/pdb9EMP/pdb
- Classification: TRANSFERASE
- Organism(s): Homo sapiens
- Expression System: Spodoptera frugiperda
- Mutation(s): No
- Deposited: 2024-03-09 Released: 2025-03-19
- Funding Organization(s): European Research Council (ERC)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.45 Å
- R-Value Free: 0.209 (Depositor), 0.209 (DCC)
- R-Value Work: 0.188 (Depositor), 0.188 (DCC)
- R-Value Observed: 0.189 (Depositor)
Starting Model: experimental
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This is version 1.0 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Probable N-acetyltransferase 16 | 334 | Homo sapiens | Mutation(s): 0 Gene Names: NAT16, C7orf52 EC: 2.3.1 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q8N8M0 (Homo sapiens) Explore Q8N8M0 Go to UniProtKB: Q8N8M0 | |||||
PHAROS: Q8N8M0 GTEx: ENSG00000167011 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q8N8M0 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| COA (Subject of Investigation/LOI) Query on COA | B [auth A] | COENZYME A C21 H36 N7 O16 P3 S RGJOEKWQDUBAIZ-IBOSZNHHSA-N |  | ||
| A1H51 (Subject of Investigation/LOI) Query on A1H51 | C [auth A] | (2~{S})-3-(1~{H}-imidazol-5-yl)-2-(tetradecanoylamino)propanoic acid C20 H35 N3 O3 OFYZXDHFDCJNGQ-SFHVURJKSA-N |  | ||
| GOL Query on GOL | D [auth A], E [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.45 Å
- R-Value Free: 0.209 (Depositor), 0.209 (DCC)
- R-Value Work: 0.188 (Depositor), 0.188 (DCC)
- R-Value Observed: 0.189 (Depositor)
Space Group: I 2 2 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 49.929 | α = 90 |
| b = 111.853 | β = 90 |
| c = 156.855 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| XDS | data reduction |
| XDS | data scaling |
| PHASER | phasing |
| Coot | model building |
Entry History & Funding Information
Deposition Data
- Released Date: 2025-03-19 Deposition Author(s): Myllykoski, M., Arnesen, T.
| Funding Organization | Location | Grant Number |
|---|---|---|
| European Research Council (ERC) | European Union | 772039 |
Revision History (Full details and data files)
- Version 1.0: 2025-03-19
Type: Initial release
