1DCN
INACTIVE MUTANT H162N OF DELTA 2 CRYSTALLIN WITH BOUND ARGININOSUCCINATE
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 | 0016829 | molecular_function | lyase activity |
| A | 0042450 | biological_process | arginine biosynthetic process via ornithine |
| 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 | 0016829 | molecular_function | lyase activity |
| B | 0042450 | biological_process | arginine biosynthetic process via ornithine |
| 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 | 0016829 | molecular_function | lyase activity |
| C | 0042450 | biological_process | arginine biosynthetic process via ornithine |
| 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 | 0016829 | molecular_function | lyase activity |
| D | 0042450 | biological_process | arginine biosynthetic process via ornithine |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AS1 D 0 |
| Chain | Residue |
| A | ASN291 |
| D | HOH508 |
| B | THR161 |
| B | ALA166 |
| D | ASN116 |
| D | ALA205 |
| D | LEU206 |
| D | TYR323 |
| D | GLN328 |
| D | LYS331 |
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 | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:11698398 |
| Chain | Residue | Details |
| A | ASN162 | |
| B | ASN162 | |
| C | ASN162 | |
| D | ASN162 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:11698398 |
| Chain | Residue | Details |
| A | SER283 | |
| B | SER283 | |
| C | SER283 | |
| D | SER283 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: in chain A => ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1K7W |
| Chain | Residue | Details |
| A | SER29 | |
| A | ASN116 | |
| B | SER29 | |
| B | ASN116 | |
| C | SER29 | |
| C | ASN116 | |
| D | SER29 | |
| D | ASN116 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: in chain C => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W |
| Chain | Residue | Details |
| A | THR161 | |
| B | THR161 | |
| C | THR161 | |
| D | THR161 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: in chain B => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W |
| Chain | Residue | Details |
| A | ASN291 | |
| B | ASN291 | |
| C | ASN291 | |
| D | ASN291 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | BINDING: in chain A => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W |
| Chain | Residue | Details |
| A | TYR323 | |
| A | LYS331 | |
| B | TYR323 | |
| B | LYS331 | |
| C | TYR323 | |
| C | LYS331 | |
| D | TYR323 | |
| D | LYS331 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | BINDING: in chain A => ECO:0000269|PubMed:10029536, ECO:0007744|PDB:1DCN |
| Chain | Residue | Details |
| A | GLN328 | |
| B | GLN328 | |
| C | GLN328 | |
| D | GLN328 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | SITE: Increases basicity of active site His => ECO:0000305|PubMed:11698398 |
| Chain | Residue | Details |
| A | GLU296 | |
| B | GLU296 | |
| C | GLU296 | |
| D | GLU296 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| D | THR161 | |
| D | ASN162 |
| site_id | CSA10 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| C | GLU296 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| D | GLU296 | |
| B | ASN162 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| C | THR161 | |
| C | ASN162 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| A | THR161 | |
| A | ASN162 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| B | THR161 | |
| B | ASN162 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| D | ASN162 | |
| B | GLU296 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| D | ASN162 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| C | ASN162 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| A | GLU296 | |
| B | ASN162 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| A | ASN162 | |
| B | GLU296 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 408 |
| Chain | Residue | Details |
| A | ASN162 | 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 | ASN162 | 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 | ASN162 | 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 | ASN162 | proton shuttle (general acid/base) |
| D | SER283 | proton shuttle (general acid/base) |
| D | LYS289 | electrostatic stabiliser |
| D | GLU296 | activator, proton shuttle (general acid/base) |
