1TJU
Crystal Structure of T161S Duck Delta 2 Crystallin Mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004056 | molecular_function | argininosuccinate lyase activity |
| A | 0005212 | molecular_function | structural constituent of eye lens |
| A | 0005829 | cellular_component | cytosol |
| A | 0006526 | biological_process | L-arginine biosynthetic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0042450 | biological_process | L-arginine biosynthetic process via ornithine |
| A | 0170033 | biological_process | L-amino acid metabolic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004056 | molecular_function | argininosuccinate lyase activity |
| B | 0005212 | molecular_function | structural constituent of eye lens |
| B | 0005829 | cellular_component | cytosol |
| B | 0006526 | biological_process | L-arginine biosynthetic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0042450 | biological_process | L-arginine biosynthetic process via ornithine |
| B | 0170033 | biological_process | L-amino acid metabolic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004056 | molecular_function | argininosuccinate lyase activity |
| C | 0005212 | molecular_function | structural constituent of eye lens |
| C | 0005829 | cellular_component | cytosol |
| C | 0006526 | biological_process | L-arginine biosynthetic process |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0042450 | biological_process | L-arginine biosynthetic process via ornithine |
| C | 0170033 | biological_process | L-amino acid metabolic process |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004056 | molecular_function | argininosuccinate lyase activity |
| D | 0005212 | molecular_function | structural constituent of eye lens |
| D | 0005829 | cellular_component | cytosol |
| D | 0006526 | biological_process | L-arginine biosynthetic process |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0042450 | biological_process | L-arginine biosynthetic process via ornithine |
| D | 0170033 | biological_process | L-amino acid metabolic process |
Functional Information from PROSITE/UniProt
| site_id | PS00163 |
| Number of Residues | 10 |
| Details | FUMARATE_LYASES Fumarate lyases signature. GSslMpQKkN |
| Chain | Residue | Details |
| A | GLY282-ASN291 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11698398","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11698398","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"in chain A","evidences":[{"source":"PubMed","id":"11698398","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1K7W","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"in chain C","evidences":[{"source":"PubMed","id":"10029536","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11698398","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DCN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K7W","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"in chain B","evidences":[{"source":"PubMed","id":"10029536","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11698398","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DCN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K7W","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"in chain A","evidences":[{"source":"PubMed","id":"10029536","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11698398","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DCN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K7W","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"in chain A","evidences":[{"source":"PubMed","id":"10029536","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DCN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Site: {"description":"Increases basicity of active site His","evidences":[{"source":"PubMed","id":"11698398","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| A | SER161 | |
| A | HIS162 | |
| B | GLU296 | |
| B | SER283 | |
| B | LYS289 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| A | GLU296 | |
| A | SER283 | |
| A | LYS289 | |
| B | SER161 | |
| B | HIS162 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| C | SER161 | |
| C | HIS162 | |
| D | GLU296 | |
| D | SER283 | |
| D | LYS289 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| C | GLU296 | |
| C | SER283 | |
| C | LYS289 | |
| D | SER161 | |
| D | HIS162 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 408 |
| Chain | Residue | Details |
| A | HIS162 | proton shuttle (general acid/base) |
| A | SER283 | proton shuttle (general acid/base) |
| A | LYS289 | electrostatic stabiliser |
| A | GLU296 | activator, proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 408 |
| Chain | Residue | Details |
| B | HIS162 | proton shuttle (general acid/base) |
| B | SER283 | proton shuttle (general acid/base) |
| B | LYS289 | electrostatic stabiliser |
| B | GLU296 | activator, proton shuttle (general acid/base) |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 408 |
| Chain | Residue | Details |
| C | HIS162 | proton shuttle (general acid/base) |
| C | SER283 | proton shuttle (general acid/base) |
| C | LYS289 | electrostatic stabiliser |
| C | GLU296 | activator, proton shuttle (general acid/base) |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 408 |
| Chain | Residue | Details |
| D | HIS162 | proton shuttle (general acid/base) |
| D | SER283 | proton shuttle (general acid/base) |
| D | LYS289 | electrostatic stabiliser |
| D | GLU296 | activator, proton shuttle (general acid/base) |
