6H9E
Structure of glutamate mutase reconstituted with homo-coenzyme B12
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 | L-glutamate catabolic process via L-citramalate |
| A | 0019670 | biological_process | anaerobic L-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 | L-glutamate catabolic process via L-citramalate |
| B | 0019670 | biological_process | anaerobic L-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 | L-glutamate catabolic process via L-citramalate |
| C | 0019670 | biological_process | anaerobic L-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 | L-glutamate catabolic process via L-citramalate |
| D | 0019670 | biological_process | anaerobic L-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 | 49 |
| Details | binding site for residue B12 A 201 |
| Chain | Residue |
| A | SER13 |
| A | LEU63 |
| A | TYR64 |
| A | GLY65 |
| A | GLY91 |
| A | GLY92 |
| A | ASN93 |
| A | VAL95 |
| A | VAL96 |
| A | GLY97 |
| A | TYR117 |
| A | ASP14 |
| A | THR121 |
| A | PRO123 |
| A | HOH315 |
| A | HOH323 |
| A | HOH326 |
| A | HOH333 |
| A | HOH343 |
| A | HOH356 |
| A | HOH360 |
| B | ILE95 |
| A | CYS15 |
| B | ALA97 |
| B | ARG100 |
| B | ASN123 |
| B | PRO180 |
| B | LEU219 |
| B | THR220 |
| B | MET294 |
| B | GLY295 |
| B | GLY296 |
| B | PHE297 |
| A | HIS16 |
| B | HIS329 |
| B | GLU330 |
| B | GLY333 |
| B | ILE334 |
| B | PRO410 |
| B | PHE471 |
| B | FWK501 |
| B | TAR502 |
| B | HOH820 |
| B | HOH865 |
| A | ALA17 |
| A | VAL18 |
| A | GLY19 |
| A | LEU23 |
| A | SER61 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue FWK B 501 |
| Chain | Residue |
| A | B12201 |
| B | ARG66 |
| B | ALA67 |
| B | GLY68 |
| B | THR94 |
| B | ASN123 |
| B | LYS326 |
| B | GLU330 |
| B | ILE334 |
| B | PRO335 |
| B | TAR502 |
| B | HOH753 |
| B | HOH793 |
| B | HOH976 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue TAR B 502 |
| Chain | Residue |
| A | B12201 |
| B | ARG66 |
| B | ARG100 |
| B | ARG149 |
| B | HIS150 |
| B | GLU171 |
| B | TYR177 |
| B | TYR181 |
| B | PHE216 |
| B | FWK501 |
| B | HOH792 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| A | LYS21 |
| B | PRO407 |
| B | PHE408 |
| B | GLY416 |
| B | MET418 |
| B | PRO420 |
| B | PHE463 |
| B | HOH624 |
| B | HOH870 |
| B | HOH941 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | GLU274 |
| B | HOH613 |
| B | HOH735 |
| B | HOH843 |
| site_id | AC6 |
| Number of Residues | 49 |
| Details | binding site for residue B12 C 201 |
| Chain | Residue |
| C | GLY91 |
| C | GLY92 |
| C | ASN93 |
| C | VAL95 |
| C | VAL96 |
| C | GLY97 |
| C | THR121 |
| C | PRO123 |
| C | HOH302 |
| C | HOH314 |
| C | HOH324 |
| C | HOH333 |
| C | HOH342 |
| C | HOH349 |
| C | HOH352 |
| C | HOH389 |
| D | ILE95 |
| D | ALA97 |
| D | ARG100 |
| D | ASN123 |
| D | PRO180 |
| D | LEU219 |
| 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 | FWK501 |
| D | TAR502 |
| D | HOH863 |
| D | HOH875 |
| C | SER13 |
| C | ASP14 |
| C | CYS15 |
| C | HIS16 |
| C | ALA17 |
| C | VAL18 |
| C | LEU23 |
| C | SER61 |
| C | LEU63 |
| C | TYR64 |
| C | GLY65 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue GOL C 202 |
| Chain | Residue |
| C | PRO123 |
| C | GLU124 |
| C | HOH323 |
| C | HOH377 |
| D | PHE471 |
| D | LYS475 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | binding site for residue FWK D 501 |
| Chain | Residue |
| C | B12201 |
| D | ARG66 |
| D | ALA67 |
| D | GLY68 |
| D | THR94 |
| D | ASN123 |
| D | LYS326 |
| D | GLU330 |
| D | ILE334 |
| D | PRO335 |
| D | TAR502 |
| D | HOH710 |
| D | HOH766 |
| D | HOH982 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | binding site for residue TAR D 502 |
| Chain | Residue |
| C | B12201 |
| D | ARG66 |
| D | ARG100 |
| D | ARG149 |
| D | HIS150 |
| D | GLU171 |
| D | TYR177 |
| D | TYR181 |
| D | PHE216 |
| D | FWK501 |
| D | HOH762 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue GOL D 503 |
| Chain | Residue |
| D | PRO407 |
| D | PHE408 |
| D | GLY416 |
| D | MET418 |
| D | MET419 |
| D | PRO420 |
| D | PHE463 |
| D | HOH612 |
| D | HOH881 |
| D | HOH900 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL D 504 |
| Chain | Residue |
| D | MET1 |
| D | GLU12 |
| D | LYS15 |
| D | GLN16 |
| D | GLU19 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 268 |
| Details | Domain: {"description":"B12-binding","evidences":[{"source":"HAMAP-Rule","id":"MF_00526","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 46 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| 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 |
