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Structure paper

TitleConformational flexibility of His200 enables catalytic activity in the T200H mutant of carbonic anhydrase II.
Journal, issue, pagesMol. Cells, Vol. 48, Page 100226-100226, Year 2025
Publish dateOct 10, 2024 (structure data deposition date)
AuthorsLim, S.W. / Jeong, H. / Kim, G.H. / Min, D. / Kim, J.K. / Kim, C.U.
External linksMol. Cells / PubMed:40441537
MethodsX-ray diffraction
Resolution1.229 - 1.287 Å
Structure data

PDB-9jwe:
Native Carbonic Anhydrase II pH 7.8 0 atm CO2
Method: X-RAY DIFFRACTION / Resolution: 1.287 Å

PDB-9jwu:
T200H Carbonic Anhydrase II pH 7.8 0 atm CO2
Method: X-RAY DIFFRACTION / Resolution: 1.229 Å

PDB-9jww:
T200H Carbonic Anhydrase II pH 7.8 20 atm CO2
Method: X-RAY DIFFRACTION / Resolution: 1.251 Å

PDB-9u5b:
T200H Carbonic Anhydrase II pH 7.8 5 atm CO2
Method: X-RAY DIFFRACTION / Resolution: 1.25 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-CO2:
CARBON DIOXIDE

ChemComp-BCT:
BICARBONATE ION / pH buffer*YM

Source
  • homo sapiens (human)
KeywordsMETAL BINDING PROTEIN / LYASE

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