Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019553 | biological_process | glutamate catabolic process via L-citramalate |
| A | 0031419 | molecular_function | cobalamin binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050096 | molecular_function | methylaspartate ammonia-lyase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019553 | biological_process | glutamate catabolic process via L-citramalate |
| B | 0031419 | molecular_function | cobalamin binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050096 | molecular_function | methylaspartate ammonia-lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 901 |
| Chain | Residue |
| A | ASP238 |
| A | GLU273 |
| A | ASP307 |
| A | HOH910 |
| A | HOH919 |
| A | HOH989 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 902 |
| Chain | Residue |
| B | HOH916 |
| B | HOH919 |
| B | HOH949 |
| B | ASP238 |
| B | GLU273 |
| B | ASP307 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 903 |
| Chain | Residue |
| A | GLU401 |
| A | ARG404 |
| A | LEU408 |
| A | HOH940 |
| A | HOH1010 |
| A | HOH1211 |
| B | HOH1097 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 904 |
| Chain | Residue |
| B | GLU401 |
| B | ARG404 |
| B | LEU408 |
| B | HOH923 |
| B | HOH1095 |
| B | HOH1303 |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | LYS331 | |
| B | LYS331 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLN172 | |
| A | THR360 | |
| B | GLN172 | |
| B | THR360 | |
| Chain | Residue | Details |
| A | ASP238 | |
| A | GLU273 | |
| A | ASP307 | |
| B | ASP238 | |
| B | GLU273 | |
| B | ASP307 | |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLN329 | |
| A | OCS361 | |
| B | GLN329 | |
| B | OCS361 | |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| A | HIS194 | |
| B | HIS194 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 11748244, 11796115 |
| Chain | Residue | Details |
| A | LYS331 | |
| A | HIS194 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 11748244, 11796115 |
| Chain | Residue | Details |
| B | LYS331 | |
| B | HIS194 | |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 468 |
| Chain | Residue | Details |
| A | GLN172 | electrostatic stabiliser |
| A | HIS194 | electrostatic stabiliser |
| A | ASP238 | metal ligand |
| A | GLU273 | metal ligand |
| A | ASP307 | metal ligand |
| A | GLN329 | electrostatic stabiliser |
| A | LYS331 | electrostatic stabiliser, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 468 |
| Chain | Residue | Details |
| B | GLN172 | electrostatic stabiliser |
| B | HIS194 | electrostatic stabiliser |
| B | ASP238 | metal ligand |
| B | GLU273 | metal ligand |
| B | ASP307 | metal ligand |
| B | GLN329 | electrostatic stabiliser |
| B | LYS331 | electrostatic stabiliser, proton acceptor, proton donor |
