3IVA
Structure of the B12-dependent Methionine Synthase (MetH) C-teminal half with AdoHcy bound
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE B12 A 1301 |
| Chain | Residue |
| A | ILE751 |
| A | ILE807 |
| A | THR808 |
| A | LEU831 |
| A | GLY833 |
| A | GLY834 |
| A | ALA835 |
| A | VAL857 |
| A | GLN858 |
| A | ASN859 |
| A | ALA860 |
| A | VAL758 |
| A | THR953 |
| A | ASP1093 |
| A | ARG1094 |
| A | GLU1097 |
| A | ALA1136 |
| A | PRO1137 |
| A | GLY1138 |
| A | TYR1139 |
| A | PRO1140 |
| A | HIS1145 |
| A | HIS759 |
| A | LYS1148 |
| A | ALA1170 |
| A | MET1171 |
| A | PRO1173 |
| A | GLY1174 |
| A | SER1176 |
| A | VAL1177 |
| A | SER1178 |
| A | SAH1401 |
| A | GLY762 |
| A | VAL766 |
| A | GLY802 |
| A | LEU803 |
| A | SER804 |
| A | LEU806 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SAH A 1401 |
| Chain | Residue |
| A | ARG823 |
| A | ASP946 |
| A | ARG1094 |
| A | GLU1097 |
| A | GLU1128 |
| A | ARG1134 |
| A | PRO1135 |
| A | ALA1136 |
| A | TYR1139 |
| A | PRO1140 |
| A | ALA1141 |
| A | TYR1189 |
| A | TYR1190 |
| A | B121301 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NO3 A 1303 |
| Chain | Residue |
| A | ASN1024 |
| A | VAL1025 |
| A | THR1150 |
| A | GLU1153 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NO3 A 1304 |
| Chain | Residue |
| A | TYR944 |
| A | GLU1105 |
| A | LEU1120 |
| A | ASN1122 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NO3 A 1305 |
| Chain | Residue |
| A | TYR1130 |
| A | GLY1132 |
| A | SER1187 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NO3 A 1306 |
| Chain | Residue |
| A | ASP911 |
| A | ASP913 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 135 |
| Details | Domain: {"description":"B12-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00666","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7992050","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BMT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"7992050","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BMT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8939751","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bmt |
| Chain | Residue | Details |
| A | SER810 | |
| A | ASP757 | |
| A | HIS759 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bmt |
| Chain | Residue | Details |
| A | LEU770 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 268 |
| Chain | Residue | Details |
| A | ASP757 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | HIS759 | hydrogen bond acceptor, hydrogen bond donor, increase electrophilicity, increase nucleophilicity, metal ligand, proton acceptor, proton donor |
| A | SER810 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
