4F5M
Wild-Type E. coli Aspartate Aminotransferase: A Template For The Interconversion of Substrate Specificity and Activity To Tyrosine Aminotransferase By The JANUS Algorithm.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| A | 0004838 | molecular_function | L-tyrosine:2-oxoglutarate aminotransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009094 | biological_process | L-phenylalanine biosynthetic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0033585 | biological_process | L-phenylalanine biosynthetic process from chorismate via phenylpyruvate |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| B | 0004838 | molecular_function | L-tyrosine:2-oxoglutarate aminotransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009094 | biological_process | L-phenylalanine biosynthetic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0033585 | biological_process | L-phenylalanine biosynthetic process from chorismate via phenylpyruvate |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 501 |
| Chain | Residue |
| A | GLY44 |
| A | TRP140 |
| A | ASN193 |
| A | LLP256 |
| A | HOH965 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO B 501 |
| Chain | Residue |
| B | ARG106 |
| B | THR107 |
| B | EDO502 |
| B | HOH622 |
| B | HOH672 |
| B | HOH700 |
| B | PRO82 |
| B | GLY85 |
| B | ARG86 |
| B | GLN89 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 502 |
| Chain | Residue |
| B | GLN89 |
| B | ILE100 |
| B | LYS103 |
| B | ARG104 |
| B | ALA105 |
| B | EDO501 |
| B | HOH831 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 503 |
| Chain | Residue |
| A | THR114 |
| A | LLP256 |
| B | TYR75 |
| B | SER294 |
| B | ASN295 |
| B | HOH937 |
Functional Information from PROSITE/UniProt
| site_id | PS00105 |
| Number of Residues | 14 |
| Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SYSKnfGLyNERVG |
| Chain | Residue | Details |
| A | SER253-GLY266 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC |
| Chain | Residue | Details |
| A | GLY44 | |
| B | GLY44 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1SPA, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC |
| Chain | Residue | Details |
| A | TRP140 | |
| B | TRP140 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1ASC, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1SPA, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC |
| Chain | Residue | Details |
| A | ASN193 | |
| B | ASN193 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0007744|PDB:1AHG, ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ARG, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC |
| Chain | Residue | Details |
| A | ARG384 | |
| B | ARG384 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11148029, ECO:0000269|PubMed:1993208, ECO:0000269|PubMed:3298240, ECO:0000269|PubMed:9891001, ECO:0007744|PDB:1AAW, ECO:0007744|PDB:1AHE, ECO:0007744|PDB:1AHF, ECO:0007744|PDB:1AHX, ECO:0007744|PDB:1AHY, ECO:0007744|PDB:1ARI, ECO:0007744|PDB:1ARS, ECO:0007744|PDB:1ASA, ECO:0007744|PDB:1ASB, ECO:0007744|PDB:1ASD, ECO:0007744|PDB:1ASE, ECO:0007744|PDB:1ASF, ECO:0007744|PDB:1ASG, ECO:0007744|PDB:1ASM, ECO:0007744|PDB:1ASN, ECO:0007744|PDB:1B4X, ECO:0007744|PDB:1CZC, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1G4V, ECO:0007744|PDB:1G4X, ECO:0007744|PDB:1G7W, ECO:0007744|PDB:1G7X, ECO:0007744|PDB:1IX6, ECO:0007744|PDB:1IX7, ECO:0007744|PDB:1IX8, ECO:0007744|PDB:1QIR, ECO:0007744|PDB:1QIS, ECO:0007744|PDB:1QIT, ECO:0007744|PDB:1YOO, ECO:0007744|PDB:2D5Y, ECO:0007744|PDB:2D61, ECO:0007744|PDB:2D63, ECO:0007744|PDB:2D7Y, ECO:0007744|PDB:3AAT, ECO:0007744|PDB:3ZZJ, ECO:0007744|PDB:5EAA |
| Chain | Residue | Details |
| A | LLP256 | |
| B | LLP256 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 777 |
| Chain | Residue | Details |
| A | TRP140 | steric role |
| A | ASP221 | proton shuttle (general acid/base) |
| A | LLP256 | proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 777 |
| Chain | Residue | Details |
| B | TRP140 | steric role |
| B | ASP221 | proton shuttle (general acid/base) |
| B | LLP256 | proton shuttle (general acid/base) |
