Extended Data Fig. 4: Methylcobalamin, MTA, SAH and SAM in Mmp10 structures.

2Fo-Fc and Fo-Fc maps of Mmp10 crystallized with SAH in the absence of peptide substrate (a: Mmp10 SAH structure). Mmp10 crystallized in the absence of substrate with SAM. Only the density of MTA was observed and labeled accordingly (b & c: Mmp10 MTA_1 and d: Mmp10 MTA_2 structures). Mmp10 crystallized with SAM and its peptide substrate (e: Mmp10 SAM peptide structure). The 2mFo-DFc map is colored blue and contoured at 1.0 σ. The mFo-DFc map is colored green (3.0 σ) and red (−3.0 σ). See Extended Data Table 1 & Fig. 2 for additional information. f, Cobalamin bound within Mmp10 (left; PDB 7QBT) and TsrM (right: PDB 6WTF). Cobalamin from TsrM shown in green and methylcobalamin from Mmp10 shown in magenta. The corrin ring and the sidechain C8 exhibit distinct conformations. g & h, Hydrophobic pocket of Mmp10 binding methylcobalamin (Mmp10 MTA_1 structure). The pocket directly beneath the cobalt of methylcobalamin has no water molecules and no charged sidechains, resulting in a hydrophobic environment. The distance between L322 and the cobalt ion is of 4 Å. Surface charge generated using APBS⁶⁶ surface charge within PyMOL (Schrödinger).