Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019553 | biological_process | L-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 | L-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 1421 |
| Chain | Residue |
| A | ASP238 |
| A | GLU273 |
| A | ASP307 |
| A | HOH2180 |
| A | HOH2181 |
| A | HOH2182 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1421 |
| Chain | Residue |
| B | HOH2182 |
| B | HOH2183 |
| B | HOH2184 |
| B | ASP238 |
| B | GLU273 |
| B | ASP307 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1416 |
| Chain | Residue |
| A | GLU401 |
| A | ARG404 |
| A | LEU408 |
| A | HOH2127 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1416 |
| Chain | Residue |
| A | HOH2060 |
| B | GLU401 |
| B | ARG404 |
| B | LEU408 |
| B | HOH2116 |
| B | HOH2256 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1417 |
| Chain | Residue |
| A | PRO10 |
| A | GLY11 |
| A | LYS49 |
| A | GLU51 |
| A | HOH2261 |
| B | ASN403 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 1417 |
| Chain | Residue |
| B | ASN199 |
| B | GLU201 |
| B | GLU202 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1418 |
| Chain | Residue |
| A | GLU308 |
| A | TRP309 |
| A | ASN311 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 1418 |
| Chain | Residue |
| A | LYS2 |
| B | ASP176 |
| B | TYR178 |
| B | ASP179 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11748244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19670200","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11748244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22614383","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer"} |
Catalytic Information from CSA
| site_id | MCSA1 |
| 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 |
