The enzyme catalyzes the protein ubiquitination. It uses a magnesium ion in two distinct steps of the reaction to bind and activate ATP PMID20797627.
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| none | none | magnesium | magnesium | mononuclear | Coordinates substrate Increases electrophilicity Electrostatic stabiliser |
*It refers to the MACiE reference pdb: 3cmm
| Metal/s Properties in Resting State | ||||||
| none | Resting state enzyme (-) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | unknownGeometry | |||||
| Coordination Number | unknown | |||||
| Notes | - | |||||
| References |
| -Rodrigo-Brenni MC, Foster SA, Morgan DO Catalysis of lysine 48-specific ubiquitin chain assembly by residues in E2 and ubiquitin. Mol Cell. 2010 Aug 27;39(4):548-59.(MEDLINE:20797627) |
| -Olsen SK, Capili AD, Lu X, Tan DS, Lima CD Active site remodelling accompanies thioester bond formation in the SUMO E1. Nature. 2010 Feb 18;463(7283):906-12.(MEDLINE:20164921) |