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Structure paper

TitleStructures of L-proline trans-hydroxylase reveal the catalytic specificity and provide deeper insight into AKG-dependent hydroxylation.
Journal, issue, pagesActa Crystallogr D Struct Biol, Vol. 79, Page 318-325, Year 2023
Publish dateOct 21, 2022 (structure data deposition date)
AuthorsHu, X. / Huang, X. / Liu, J. / Zheng, P. / Gong, W. / Yang, L.
External linksActa Crystallogr D Struct Biol / PubMed:36974966
MethodsX-ray diffraction
Resolution1.84 - 2.38 Å
Structure data

PDB-8h7t:
Trans-3/4-proline-hydroxylase H11 apo structure
Method: X-RAY DIFFRACTION / Resolution: 1.88 Å

PDB-8h7v:
Trans-3/4-proline-hydroxylase H11 with AKG
Method: X-RAY DIFFRACTION / Resolution: 1.97 Å

PDB-8h7y:
Trans-3/4-proline-hydroxylase H11 with AKG and L-proline
Method: X-RAY DIFFRACTION / Resolution: 2.14 Å

PDB-8h81:
Trans-3/4-proline-hydroxylase H11 with 4-Hydroxyl-proline
Method: X-RAY DIFFRACTION / Resolution: 1.84 Å

PDB-8h85:
Trans-3/4-proline-hydroxylase H11 with 3-hydroxyl-proline
Method: X-RAY DIFFRACTION / Resolution: 2.38 Å

Chemicals

ChemComp-CL:
Unknown entry / Chloride

ChemComp-HOH:
WATER / Water

ChemComp-AKG:
2-OXOGLUTARIC ACID / Α-Ketoglutaric acid

ChemComp-FE:
Unknown entry / Iron

ChemComp-PRO:
PROLINE / Proline

ChemComp-HYP:
4-HYDROXYPROLINE / Hydroxyproline

ChemComp-HY3:
3-HYDROXYPROLINE / Hydroxyproline

Source
  • uncultured bacterium esnapd13 (environmental samples)
KeywordsSTRUCTURAL PROTEIN / L-proline / Trans / Hydroxylase / AKG / HYDROLASE

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