3-hydroxypropionate--CoA ligase [ADP-forming]
Nitrosopumilus maritimus SCM1
State in the Current Structure
| Assembly | Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Associated Components | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|
| 1 | Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count | Chain A； UniProt 1–705 Chain B； UniProt 1–705 | Not recorded | ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 3OH 3-HYDROXY-PROPANOIC ACID × 2 PO4 PHOSPHATE ION × 2 MG MAGNESIUM ION × 1 | X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；298 K；200 mM Magnesium chloride hexahydrate, 100 mM Tris pH 8.5, 7% (v/v) PEG 6000 | Resolution 2.80 Å R-free 0.254 |
Other States of the Same Protein in the Database
Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.
No other PDB entry for the same UniProt protein was found.
View Construct and Data Evidence
| UniProt name | HPCAL_NITMS |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–705； UniProt 1–705 Author chain B； PDBConstruct 1–705； UniProt 1–705 |
