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-Structure paper
| Title | The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex. |
|---|---|
| Journal, issue, pages | Febs Lett., Vol. 583, Page 585-590, Year 2009 |
| Publish date | Oct 31, 2008 (structure data deposition date) |
Authors | Hiromoto, T. / Ataka, K. / Pilak, O. / Vogt, S. / Stagni, M.S. / Meyer-Klaucke, W. / Warkentin, E. / Thauer, R.K. / Shima, S. / Ermler, U. |
External links | Febs Lett. / PubMed:19162018 |
| Methods | X-ray diffraction |
| Resolution | 1.75 - 1.95 Å |
| Structure data | ![]() PDB-3f46: ![]() PDB-3f47: |
| Chemicals | ![]() ChemComp-I2C: ![]() ChemComp-FE2: ![]() ChemComp-CMO: ![]() ChemComp-DTV: ![]() ChemComp-HOH: ![]() ChemComp-NA: |
| Source |
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Keywords | OXIDOREDUCTASE / ROSSMANN FOLD / HELIX BUNDLE / COMPLEX WITH IRON GUANYLYL PYRIDINOL COFACTOR / C176A MUTANT / Methanogenesis / One-carbon metabolism |
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methanocaldococcus jannaschii (archaea)
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