Download MendeleyStructure of ALAS bound to succinyl-CoA from S. cerevisiae
Tran, J.U., Brown, B.L.To be published.
9DZO | pdb_00009dzo
Structure of ALAS bound to succinyl-CoA from S. cerevisiae
- PDB DOI: https://doi.org/10.2210/pdb9DZO/pdb
- Classification: TRANSFERASE
- Organism(s): Saccharomyces cerevisiae
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2024-10-16 Released: 2025-10-22
- Funding Organization(s): National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS), American Heart Association
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.69 Å
- R-Value Free: 0.227 (Depositor), 0.231 (DCC)
- R-Value Work: 0.180 (Depositor), 0.186 (DCC)
Starting Model: experimental
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This is version 1.0 of the entry. See complete history.
Literature
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| 5-aminolevulinate synthase, mitochondrial | A [auth C], B [auth D], C [auth A], D [auth E], E [auth B] | 491 | Saccharomyces cerevisiae | Mutation(s): 0 Gene Names: HEM1, CYD1, YDR232W, YD9934.16 EC: 2.3.1.37 |  |
UniProt | |||||
Find proteins for P09950 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore P09950 Go to UniProtKB: P09950 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P09950 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| 5-aminolevulinate synthase, mitochondrial | 491 | Saccharomyces cerevisiae | Mutation(s): 0 Gene Names: HEM1, CYD1, YDR232W, YD9934.16 EC: 2.3.1.37 |  | |
UniProt | |||||
Find proteins for P09950 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore P09950 Go to UniProtKB: P09950 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P09950 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| SCA (Subject of Investigation/LOI) Query on SCA | H [auth C], L [auth A], N [auth E], P [auth B], Q [auth F] | SUCCINYL-COENZYME A C25 H40 N7 O19 P3 S VNOYUJKHFWYWIR-ITIYDSSPSA-N |  | ||
| PLP (Subject of Investigation/LOI) Query on PLP | G [auth C], I [auth D], K [auth A], M [auth E], O [auth B] | PYRIDOXAL-5'-PHOSPHATE C8 H10 N O6 P NGVDGCNFYWLIFO-UHFFFAOYSA-N |  | ||
| MG Query on MG | J [auth D] | MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| LLP Query on LLP | F | L-PEPTIDE LINKING | C14 H22 N3 O7 P |  | LYS |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.69 Å
- R-Value Free: 0.227 (Depositor), 0.231 (DCC)
- R-Value Work: 0.180 (Depositor), 0.186 (DCC)
Space Group: P 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 60.595 | α = 116.403 |
| b = 114.241 | β = 97.507 |
| c = 119.307 | γ = 91.839 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| XDS | data reduction |
| XDS | data scaling |
| PHASER | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2025-10-22 Deposition Author(s): Tran, J.U., Brown, B.L.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | United States | DP2 GM146255 |
| American Heart Association | United States | 24PRE1190012 |
Revision History (Full details and data files)
- Version 1.0: 2025-10-22
Type: Initial release
