Download MendeleyThe Protein Complex NatA Binds Inositol Hexakisphosphate and Exhibits Conformational Flexibility
Neubauer, J.L., Pham, T., Immormino, R.M., Dollins, D.E., Endo-Streeter, S.T., Li, S., Pemble IV, C.W., York, J.D.To be published.
4HNY | pdb_00004hny
Apo N-terminal acetyltransferase complex A
- PDB DOI: https://doi.org/10.2210/pdb4HNY/pdb
- Classification: TRANSFERASE
- Organism(s): Saccharomyces cerevisiae S288C
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2012-10-21 Released: 2014-03-26
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.25 Å
- R-Value Free: 0.220 (Depositor), 0.221 (DCC)
- R-Value Work: 0.178 (Depositor), 0.182 (DCC)
- R-Value Observed: 0.179 (Depositor)
wwPDB Validation 3D Report Full Report
This is version 1.1 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 |
| N-terminal acetyltransferase A complex subunit NAT1 | 863 | Saccharomyces cerevisiae S288C | Mutation(s): 0 Gene Names: NAT1, AAA1, YDL040C, D2720 |  | |
UniProt | |||||
Find proteins for P12945 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore P12945 Go to UniProtKB: P12945 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P12945 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| N-terminal acetyltransferase A complex catalytic subunit ARD1 | 248 | Saccharomyces cerevisiae S288C | Mutation(s): 0 Gene Names: ARD1, YHR013C EC: 2.3.1.88 (PDB Primary Data), 2.3.1.255 (UniProt) |  | |
UniProt | |||||
Find proteins for P07347 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore P07347 Go to UniProtKB: P07347 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P07347 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PG4 Query on PG4 | E [auth A] F [auth A] H [auth B] I [auth B] J [auth B] | TETRAETHYLENE GLYCOL C8 H18 O5 UWHCKJMYHZGTIT-UHFFFAOYSA-N |  | ||
| GOL Query on GOL | G [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.25 Å
- R-Value Free: 0.220 (Depositor), 0.221 (DCC)
- R-Value Work: 0.178 (Depositor), 0.182 (DCC)
- R-Value Observed: 0.179 (Depositor)
Space Group: P 31
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 129.416 | α = 90 |
| b = 129.416 | β = 90 |
| c = 171.783 | γ = 120 |
| Software Name | Purpose |
|---|---|
| HKL-2000 | data collection |
| PHENIX | model building |
| PHENIX | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| PHENIX | phasing |
Entry History
Deposition Data
- Released Date: 2014-03-26 Deposition Author(s): Neubauer, J.L., Immormino, R.M., Dollins, D.E., Endo-Streeter, S.T., Pemble IV, C.W., York, J.D.
Revision History (Full details and data files)
- Version 1.0: 2014-03-26
Type: Initial release - Version 1.1: 2024-11-06
Changes: Data collection, Database references, Derived calculations, Structure summary
