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 | 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
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 | CYS361 | |
B | GLN329 | |
B | CYS361 | |
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 | 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 | 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 |