1I9C
GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM: COMPLEX WITH ADENOSYLCOBALAMIN AND SUBSTRATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016866 | molecular_function | intramolecular transferase activity |
| A | 0019553 | biological_process | glutamate catabolic process via L-citramalate |
| A | 0019670 | biological_process | anaerobic glutamate catabolic process |
| A | 0031419 | molecular_function | cobalamin binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050097 | molecular_function | methylaspartate mutase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016866 | molecular_function | intramolecular transferase activity |
| B | 0019553 | biological_process | glutamate catabolic process via L-citramalate |
| B | 0019670 | biological_process | anaerobic glutamate catabolic process |
| B | 0031419 | molecular_function | cobalamin binding |
| B | 0050097 | molecular_function | methylaspartate mutase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0016866 | molecular_function | intramolecular transferase activity |
| C | 0019553 | biological_process | glutamate catabolic process via L-citramalate |
| C | 0019670 | biological_process | anaerobic glutamate catabolic process |
| C | 0031419 | molecular_function | cobalamin binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050097 | molecular_function | methylaspartate mutase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0016866 | molecular_function | intramolecular transferase activity |
| D | 0019553 | biological_process | glutamate catabolic process via L-citramalate |
| D | 0019670 | biological_process | anaerobic glutamate catabolic process |
| D | 0031419 | molecular_function | cobalamin binding |
| D | 0050097 | molecular_function | methylaspartate mutase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 46 |
| Details | BINDING SITE FOR RESIDUE B12 A 800 |
| Chain | Residue |
| A | SER13 |
| A | SER61 |
| A | LEU63 |
| A | TYR64 |
| A | GLY65 |
| A | GLY91 |
| A | GLY92 |
| A | ASN93 |
| A | VAL95 |
| A | VAL96 |
| A | GLY97 |
| A | ASP14 |
| A | THR121 |
| A | HOH804 |
| A | HOH806 |
| A | HOH807 |
| A | HOH809 |
| A | HOH814 |
| A | HOH816 |
| A | HOH855 |
| B | ILE95 |
| B | ALA97 |
| A | CYS15 |
| B | ARG100 |
| B | ASN123 |
| B | PRO180 |
| B | LEU219 |
| B | THR220 |
| B | MET294 |
| B | GLY295 |
| B | GLY296 |
| B | PHE297 |
| B | HIS329 |
| A | HIS16 |
| B | GLU330 |
| B | GLY333 |
| B | ILE334 |
| B | PHE471 |
| B | 5AD1303 |
| B | GLU1305 |
| B | HOH1363 |
| A | ALA17 |
| A | VAL18 |
| A | GLY19 |
| A | ILE22 |
| A | LEU23 |
| site_id | AC2 |
| Number of Residues | 48 |
| Details | BINDING SITE FOR RESIDUE B12 C 800 |
| Chain | Residue |
| C | SER13 |
| C | ASP14 |
| C | CYS15 |
| C | HIS16 |
| C | ALA17 |
| C | VAL18 |
| C | GLY19 |
| C | LEU23 |
| C | SER61 |
| C | LEU63 |
| C | TYR64 |
| C | GLY65 |
| C | GLY91 |
| C | GLY92 |
| C | ASN93 |
| C | VAL95 |
| C | VAL96 |
| C | GLY97 |
| C | THR121 |
| C | PRO123 |
| C | HOH801 |
| C | HOH805 |
| C | HOH808 |
| C | HOH809 |
| C | HOH813 |
| C | HOH817 |
| C | HOH833 |
| D | ILE95 |
| D | ALA97 |
| D | ARG100 |
| D | ASN123 |
| D | PRO180 |
| D | THR220 |
| D | MET294 |
| D | GLY295 |
| D | GLY296 |
| D | PHE297 |
| D | HIS329 |
| D | GLU330 |
| D | ALA331 |
| D | GLY333 |
| D | ILE334 |
| D | PRO410 |
| D | PHE471 |
| D | 5AD1304 |
| D | GLU1306 |
| D | 2AS1308 |
| D | HOH1361 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 5AD B 1303 |
| Chain | Residue |
| B | ASN123 |
| B | LYS326 |
| B | GLU330 |
| B | ILE334 |
| B | PRO335 |
| B | GLU1305 |
| B | 2AS1307 |
| B | HOH1330 |
| B | HOH1335 |
| B | HOH1378 |
| B | HOH1436 |
| A | B12800 |
| B | ARG66 |
| B | ALA67 |
| B | GLY68 |
| B | THR94 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 5AD D 1304 |
| Chain | Residue |
| C | B12800 |
| D | ARG66 |
| D | ALA67 |
| D | GLY68 |
| D | THR94 |
| D | ASN123 |
| D | LYS326 |
| D | GLU330 |
| D | ILE334 |
| D | PRO335 |
| D | GLU1306 |
| D | 2AS1308 |
| D | HOH1314 |
| D | HOH1322 |
| D | HOH1380 |
| D | HOH1454 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE GLU B 1305 |
| Chain | Residue |
| A | B12800 |
| B | ARG66 |
| B | THR94 |
| B | ARG100 |
| B | ARG149 |
| B | HIS150 |
| B | GLU171 |
| B | TYR177 |
| B | TYR181 |
| B | PHE216 |
| B | HIS291 |
| B | 5AD1303 |
| B | HOH1315 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 2AS B 1307 |
| Chain | Residue |
| B | ARG66 |
| B | THR94 |
| B | ARG100 |
| B | ARG149 |
| B | HIS150 |
| B | GLU171 |
| B | TYR177 |
| B | TYR181 |
| B | PHE216 |
| B | HIS291 |
| B | 5AD1303 |
| B | HOH1315 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE GLU D 1306 |
| Chain | Residue |
| C | B12800 |
| D | ARG66 |
| D | THR94 |
| D | ARG100 |
| D | ARG149 |
| D | HIS150 |
| D | GLU171 |
| D | TYR177 |
| D | TYR181 |
| D | PHE216 |
| D | HIS291 |
| D | 5AD1304 |
| D | HOH1325 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 2AS D 1308 |
| Chain | Residue |
| C | B12800 |
| D | ARG66 |
| D | ARG100 |
| D | ARG149 |
| D | HIS150 |
| D | GLU171 |
| D | TYR177 |
| D | TYR181 |
| D | PHE216 |
| D | HIS291 |
| D | 5AD1304 |
| D | HOH1325 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 26 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | ARG66 | |
| B | PHE297 | |
| B | LYS326 | |
| B | GLU330 | |
| B | ILE334 | |
| D | ARG66 | |
| D | GLY68 | |
| D | ARG100 | |
| D | ASN123 | |
| D | ARG149 | |
| D | GLU171 | |
| B | GLY68 | |
| D | TYR177 | |
| D | PRO180 | |
| D | TYR181 | |
| D | PHE297 | |
| D | LYS326 | |
| D | GLU330 | |
| D | ILE334 | |
| B | ARG100 | |
| B | ASN123 | |
| B | ARG149 | |
| B | GLU171 | |
| B | TYR177 | |
| B | PRO180 | |
| B | TYR181 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | HIS16 | |
| C | HIS16 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bmt |
| Chain | Residue | Details |
| A | ASP14 | |
| A | HIS16 | |
| A | GLY67 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bmt |
| Chain | Residue | Details |
| C | ASP14 | |
| C | HIS16 | |
| C | GLY67 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bmt |
| Chain | Residue | Details |
| B | GLU171 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bmt |
| Chain | Residue | Details |
| D | GLU171 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bmt |
| Chain | Residue | Details |
| A | PHE27 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bmt |
| Chain | Residue | Details |
| C | PHE27 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 63 |
| Chain | Residue | Details |
| B | ARG100 | electrostatic stabiliser |
| B | GLU171 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 63 |
| Chain | Residue | Details |
| D | ARG100 | electrostatic stabiliser |
| D | GLU171 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
