2Q7W
Structural Studies Reveals the Inactivation of E. coli L-aspartate aminotransferase (S)-4,5-amino-dihydro-2-thiophenecarboxylic acid (SADTA) via two mechanisms at pH 6.0
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 transaminase 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 | 0016740 | molecular_function | transferase activity |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 500 |
| Chain | Residue |
| A | LYS121 |
| A | ARG122 |
| A | ARG360 |
| A | HOH1161 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PSZ A 600 |
| Chain | Residue |
| A | TRP130 |
| A | ASN183 |
| A | ASP211 |
| A | TYR214 |
| A | SER243 |
| A | SER245 |
| A | KST246 |
| A | ARG254 |
| A | PHE348 |
| A | ARG374 |
| A | GOL810 |
| A | HOH817 |
| A | HOH980 |
| A | ILE33 |
| A | GLY34 |
| A | TYR65 |
| A | GLY103 |
| A | THR104 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PMP A 700 |
| Chain | Residue |
| A | TYR65 |
| A | GLY103 |
| A | THR104 |
| A | TRP130 |
| A | ASN183 |
| A | ASP211 |
| A | TYR214 |
| A | SER243 |
| A | SER245 |
| A | KST246 |
| A | ARG254 |
| A | HOH817 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 801 |
| Chain | Residue |
| A | LYS134 |
| A | ASN138 |
| A | GLU143 |
| A | VAL144 |
| A | ARG145 |
| A | GOL808 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 802 |
| Chain | Residue |
| A | GLY216 |
| A | GLY220 |
| A | LEU221 |
| A | GLU308 |
| A | LEU311 |
| A | THR312 |
| A | ARG315 |
| A | GOL809 |
| A | HOH1112 |
| A | HOH1179 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 803 |
| Chain | Residue |
| A | PRO72 |
| A | ARG76 |
| A | HOH898 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 804 |
| Chain | Residue |
| A | TYR36 |
| A | THR43 |
| A | PRO44 |
| A | LEU46 |
| A | KST246 |
| A | GLY249 |
| A | TYR251 |
| A | MET314 |
| A | HOH1187 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 805 |
| Chain | Residue |
| A | PRO72 |
| A | GLY75 |
| A | ARG76 |
| A | GLN79 |
| A | ARG96 |
| A | THR97 |
| A | HOH812 |
| A | HOH990 |
| A | HOH1132 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 806 |
| Chain | Residue |
| A | HIS155 |
| A | GLY186 |
| A | ILE187 |
| A | ASP188 |
| A | LYS343 |
| A | GLN344 |
| A | HOH876 |
| A | HOH1125 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 807 |
| Chain | Residue |
| A | ARG315 |
| A | GLN316 |
| A | GLN319 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 808 |
| Chain | Residue |
| A | ASN138 |
| A | GLY141 |
| A | LEU142 |
| A | GLU143 |
| A | GOL801 |
| A | HOH931 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 809 |
| Chain | Residue |
| A | GLY220 |
| A | LEU221 |
| A | GLU222 |
| A | GLU223 |
| A | GOL802 |
| A | HOH1110 |
| A | HOH1179 |
| site_id | BC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 810 |
| Chain | Residue |
| A | SER284 |
| A | ASN285 |
| A | PSZ600 |
| A | HOH817 |
| A | HOH874 |
| A | HOH1042 |
| A | ILE33 |
| A | TYR65 |
| A | KST246 |
| A | ARG280 |
| site_id | BC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 811 |
| Chain | Residue |
| A | ILE33 |
| A | VAL35 |
| A | LYS37 |
| A | ASN64 |
| A | HOH963 |
| A | HOH1010 |
| A | HOH1042 |
| A | HOH1173 |
| A | HOH1231 |
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 | SER243-GLY256 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC |
| Chain | Residue | Details |
| A | GLY34 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| 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 | TRP130 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| 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 | ASN183 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| 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 | ARG374 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| 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 | KST246 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP211 | |
| A | TRP130 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ILE68 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 777 |
| Chain | Residue | Details |
| A | TRP130 | steric role |
| A | ASP211 | proton shuttle (general acid/base) |
| A | KST246 | proton shuttle (general acid/base) |
