2QBT
Structural Studies Reveal The Inactivation of E. coli L-aspartate aminotransferase by (S)-4,5-amino-dihydro-2-thiophenecarboxylic acid (SADTA) via Two Mechanisms (at pH 8.0)
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 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 501 |
Chain | Residue |
A | LYS134 |
A | ASN138 |
A | GLU143 |
A | VAL144 |
A | ARG145 |
A | GOL806 |
A | HOH1121 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 502 |
Chain | Residue |
A | HOH894 |
A | PRO72 |
A | ARG76 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 503 |
Chain | Residue |
A | THR312 |
A | ARG315 |
A | GLN316 |
A | GOL804 |
A | HOH941 |
site_id | AC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE PSZ A 600 |
Chain | Residue |
A | GLY34 |
A | TYR65 |
A | GLY102 |
A | GLY103 |
A | THR104 |
A | TRP130 |
A | ASN183 |
A | ASP211 |
A | TYR214 |
A | SER243 |
A | SER245 |
A | KST246 |
A | ARG254 |
A | PHE348 |
A | ARG374 |
A | GOL808 |
A | HOH1021 |
A | HOH1206 |
site_id | AC5 |
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 | HOH814 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 801 |
Chain | Residue |
A | GLY216 |
A | GLY220 |
A | LEU221 |
A | GLU308 |
A | THR312 |
A | ARG315 |
A | HOH1085 |
A | HOH1199 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 802 |
Chain | Residue |
A | TYR36 |
A | THR43 |
A | PRO44 |
A | LEU46 |
A | KST246 |
A | GLY249 |
A | TYR251 |
A | MET314 |
A | HOH1192 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 803 |
Chain | Residue |
A | PRO72 |
A | GLY75 |
A | ARG76 |
A | GLN79 |
A | ALA95 |
A | ARG96 |
A | THR97 |
A | HOH809 |
A | HOH1103 |
A | HOH1140 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 804 |
Chain | Residue |
A | ARG315 |
A | GLN316 |
A | GLN319 |
A | SO4503 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 805 |
Chain | Residue |
A | TYR55 |
A | ASN300 |
A | LEU303 |
A | HOH966 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 806 |
Chain | Residue |
A | ASN138 |
A | GLY141 |
A | LEU142 |
A | SO4501 |
site_id | BC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 807 |
Chain | Residue |
A | PRO189 |
A | THR190 |
A | LEU191 |
A | ARG219 |
A | ASN345 |
A | HOH833 |
A | HOH855 |
A | HOH918 |
A | HOH1001 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 808 |
Chain | Residue |
A | HOH1190 |
A | TYR65 |
A | KST246 |
A | ARG280 |
A | PSZ600 |
A | HOH1024 |
A | HOH1163 |
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) |