Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0009236 | biological_process | cobalamin biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0032259 | biological_process | methylation |
A | 0046026 | molecular_function | precorrin-4 C11-methyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PO4 A 400 |
Chain | Residue |
A | PRO16 |
A | ARG17 |
A | GLY18 |
A | SER19 |
A | HIS20 |
A | GLY160 |
A | ARG161 |
A | THR162 |
A | HOH574 |
A | HOH576 |
A | HOH577 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 401 |
Chain | Residue |
A | HIS100 |
A | THR101 |
A | GLY108 |
A | HOH504 |
A | HOH613 |
site_id | AC3 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE SAH A 300 |
Chain | Residue |
A | PRO30 |
A | THR101 |
A | GLY102 |
A | ASP103 |
A | MET106 |
A | THR131 |
A | SER132 |
A | PHE183 |
A | LEU184 |
A | VAL210 |
A | LYS212 |
A | ALA213 |
A | GLN240 |
A | ALA241 |
A | MET242 |
A | HOH504 |
A | HOH509 |
A | HOH519 |
site_id | P-4 |
Number of Residues | 7 |
Details | PRECORRIN-4 BINDING SITE IN DEEP TROUGH. ALSO, LOCATION OF BOUND PHOSPHATE RESIDUE 401. PHOSPHATE PRESENT FROM CRYSTALLIZATION CONDITIONS. |
Chain | Residue |
A | PO4401 |
A | ALA53 |
A | SER55 |
A | LEU79 |
A | ARG98 |
A | GLU112 |
A | GLN113 |
site_id | PAL |
Number of Residues | 1 |
Details | PHOSPHATE ION INVOLVED IN CRYSTAL CONTACT. |
site_id | SAH |
Number of Residues | 1 |
Details | S-ADENOSYL-HOMOCYSTEINE BINDING SITE. CRYSTALS FORMED IN THE PRESENCE OF ADOMET OR ADOHCY. |
Functional Information from PROSITE/UniProt
site_id | PS00839 |
Number of Residues | 15 |
Details | SUMT_1 Uroporphyrin-III C-methyltransferase signature 1. IGAGPGdpdLITVKG |
Chain | Residue | Details |
A | ILE26-GLY40 | |