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 | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 701 |
| Chain | Residue |
| A | GLU401 |
| A | ARG404 |
| A | HOH719 |
| A | HOH737 |
| A | HOH992 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 702 |
| Chain | Residue |
| B | GLU401 |
| B | ARG404 |
| B | HOH727 |
| B | HOH749 |
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 | 4 |
| 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 | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kcz |
| Chain | Residue | Details |
| A | LYS331 | |
| A | HIS194 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kcz |
| Chain | Residue | Details |
| B | LYS331 | |
| B | HIS194 | |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 468 |
| Chain | Residue | Details |
| A | GLU188 | electrostatic stabiliser |
| A | TYR214 | electrostatic stabiliser |
| A | ILE258 | metal ligand |
| A | GLY297 | metal ligand |
| A | ASP343 | metal ligand |
| A | GLU369 | electrostatic stabiliser |
| A | THR371 | electrostatic stabiliser, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 468 |
| Chain | Residue | Details |
| B | GLU188 | electrostatic stabiliser |
| B | TYR214 | electrostatic stabiliser |
| B | ILE258 | metal ligand |
| B | GLY297 | metal ligand |
| B | ASP343 | metal ligand |
| B | GLU369 | electrostatic stabiliser |
| B | THR371 | electrostatic stabiliser, proton acceptor, proton donor |
