EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.14.18.3 | crystal structure analysis, PDB ID 3CHX, structure modeling | Methylosinus trichosporium |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.14.18.3 | membrane | - |
Methylosinus trichosporium | 16020 | - |
1.14.18.3 | membrane | - |
Methylocystis sp. | 16020 | - |
1.14.18.3 | membrane | - |
Methylococcus capsulatus | 16020 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.18.3 | Cu2+ | a metal centre in subunit-C, and not subunit-B, is essential for copper-containing membrane monooxygenase activity | Methylosinus trichosporium | |
1.14.18.3 | Cu2+ | a metal centre in subunit-C, and not subunit-B, is essential for copper-containing membrane monooxygenase activity | Methylocystis sp. | |
1.14.18.3 | Cu2+ | two metal sites: a dicopper centre coordinated by histidine residues in subunit-B and a variable-metal site coordinated by carboxylate and histidine residues from subunit-C. A metal centre in subunit-C, and not subunit-B, is essential for copper-containing membrane monooxygenase activity | Methylococcus capsulatus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.18.3 | Methylococcus capsulatus | G1UBD1 AND Q607G3 | alpha- and beta-subunits | - |
1.14.18.3 | Methylococcus capsulatus Bath | G1UBD1 AND Q607G3 | alpha- and beta-subunits | - |
1.14.18.3 | Methylocystis sp. | - |
- |
- |
1.14.18.3 | Methylosinus trichosporium | - |
- |
- |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.14.18.3 | More | enzyme structure comparisons, overview | Methylosinus trichosporium |
1.14.18.3 | More | enzyme structure comparisons, overview | Methylocystis sp. |
1.14.18.3 | More | enzyme structure comparisons, overview | Methylococcus capsulatus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.18.3 | copper-containing membrane monooxygenase | - |
Methylosinus trichosporium |
1.14.18.3 | copper-containing membrane monooxygenase | - |
Methylocystis sp. |
1.14.18.3 | copper-containing membrane monooxygenase | - |
Methylococcus capsulatus |
1.14.18.3 | particulate methane monooxygenase | - |
Methylosinus trichosporium |
1.14.18.3 | particulate methane monooxygenase | - |
Methylocystis sp. |
1.14.18.3 | particulate methane monooxygenase | - |
Methylococcus capsulatus |
1.14.18.3 | pMMO | - |
Methylosinus trichosporium |
1.14.18.3 | pMMO | - |
Methylocystis sp. |
1.14.18.3 | pMMO | - |
Methylococcus capsulatus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.14.18.3 | evolution | the enzyme is a member of the copper-containing membrane monooxygenase (CuMMO) superfamily | Methylosinus trichosporium |
1.14.18.3 | evolution | the enzyme is a member of the copper-containing membrane monooxygenase (CuMMO) superfamily | Methylocystis sp. |
1.14.18.3 | evolution | the enzyme is a member of the copper-containing membrane monooxygenase (CuMMO) superfamily | Methylococcus capsulatus |
1.14.18.3 | additional information | structure-function relationship of copper-containing membrane monooxygenases | Methylosinus trichosporium |
1.14.18.3 | additional information | structure-function relationship of copper-containing membrane monooxygenases | Methylocystis sp. |
1.14.18.3 | additional information | structure-function relationship of copper-containing membrane monooxygenases | Methylococcus capsulatus |