1K7Y
E. coli MetH C-terminal fragment (649-1227)
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 254 |
Chain | Residue |
A | LYS712 |
A | HIS927 |
A | ARG928 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 255 |
Chain | Residue |
A | SO4282 |
A | LYS755 |
A | PRO785 |
A | ALA786 |
A | GLU787 |
A | ASN816 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 267 |
Chain | Residue |
A | ARG928 |
A | GLN932 |
A | ARG1106 |
A | TYR1111 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 323 |
Chain | Residue |
A | TYR1139 |
A | B121248 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 251 |
Chain | Residue |
A | LYS720 |
A | ARG723 |
A | TYR1083 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 259 |
Chain | Residue |
A | LYS819 |
A | LYS1188 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 260 |
Chain | Residue |
A | ARG823 |
A | PRO1140 |
A | B121248 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 270 |
Chain | Residue |
A | ARG996 |
A | HIS1160 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 282 |
Chain | Residue |
A | SO4255 |
A | ARG1127 |
site_id | BC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 A 309 |
Chain | Residue |
A | VAL971 |
site_id | BC2 |
Number of Residues | 38 |
Details | BINDING SITE FOR RESIDUE B12 A 1248 |
Chain | Residue |
A | SO4260 |
A | HOH271 |
A | HOH279 |
A | SO4323 |
A | VAL758 |
A | GLY762 |
A | ILE765 |
A | VAL766 |
A | GLY802 |
A | LEU803 |
A | SER804 |
A | LEU806 |
A | ILE807 |
A | THR808 |
A | LEU831 |
A | GLY833 |
A | GLY834 |
A | ALA835 |
A | THR836 |
A | VAL857 |
A | GLN858 |
A | ASN859 |
A | ALA860 |
A | THR863 |
A | ASP1093 |
A | ALA1136 |
A | PRO1137 |
A | GLY1138 |
A | TYR1139 |
A | PRO1140 |
A | HIS1145 |
A | ALA1170 |
A | MET1171 |
A | GLY1174 |
A | ALA1175 |
A | SER1176 |
A | VAL1177 |
A | SER1178 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000269|PubMed:7992050, ECO:0007744|PDB:1BMT |
Chain | Residue | Details |
A | GLU694 | |
A | GLY756 | |
A | SER804 | |
A | THR808 | |
A | ALA860 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: axial binding residue => ECO:0000269|PubMed:7992050, ECO:0007744|PDB:1BMT |
Chain | Residue | Details |
A | GLY759 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8939751 |
Chain | Residue | Details |
A | ASP946 | |
A | ARG1134 | |
A | TYR1189 |
Catalytic Information from CSA
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 | GLY759 | 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 |
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bmt |
Chain | Residue | Details |
A | SER810 | |
A | ASP757 | |
A | GLY759 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1bmt |
Chain | Residue | Details |
A | LEU770 |