2QB2
Structural Studies Reveal the Inactivation of E. coli L-aspartate aminotransferase by (s)-4,5-dihydro-2thiophenecarboylic acid (SADTA) via two mechanisms (at pH 7.0).
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 1001 |
| Chain | Residue |
| A | PRO72 |
| A | ARG76 |
| A | HOH1088 |
| A | HOH1317 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1002 |
| Chain | Residue |
| A | HOH1281 |
| A | THR312 |
| A | ARG315 |
| A | GOL705 |
| A | GOL900 |
| A | HOH1132 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PSZ A 600 |
| Chain | Residue |
| A | ILE33 |
| A | GLY34 |
| A | TYR65 |
| A | GLY103 |
| A | THR104 |
| A | TRP130 |
| A | ASN183 |
| A | ASP211 |
| A | ALA213 |
| A | TYR214 |
| A | SER243 |
| A | SER245 |
| A | KST246 |
| A | ARG254 |
| A | PHE348 |
| A | ARG374 |
| A | GOL902 |
| A | HOH1008 |
| A | HOH1166 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PMP A 700 |
| Chain | Residue |
| 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 | HOH1008 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 701 |
| Chain | Residue |
| A | LYS134 |
| A | ASN138 |
| A | GLU143 |
| A | VAL144 |
| A | GOL708 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 702 |
| Chain | Residue |
| A | GLY216 |
| A | GLY220 |
| A | LEU221 |
| A | GLU308 |
| A | LEU311 |
| A | THR312 |
| A | ARG315 |
| A | GOL900 |
| A | HOH1281 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE GOL A 703 |
| Chain | Residue |
| A | TYR36 |
| A | THR43 |
| A | PRO44 |
| A | LEU46 |
| A | KST246 |
| A | PHE248 |
| A | GLY249 |
| A | TYR251 |
| A | GLU310 |
| A | MET314 |
| A | HOH1044 |
| A | HOH1103 |
| A | HOH1170 |
| A | HOH1224 |
| A | HOH1270 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GOL A 704 |
| Chain | Residue |
| A | PRO72 |
| A | GLY75 |
| A | ARG76 |
| A | GLN79 |
| A | ALA95 |
| A | ARG96 |
| A | THR97 |
| A | HOH1003 |
| A | HOH1036 |
| A | HOH1074 |
| A | HOH1297 |
| A | HOH1358 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 705 |
| Chain | Residue |
| A | ALA218 |
| A | ARG315 |
| A | GLN316 |
| A | GLN319 |
| A | SO41002 |
| A | HOH1070 |
| A | HOH1072 |
| A | HOH1235 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 706 |
| Chain | Residue |
| A | ASN4 |
| A | TYR150 |
| A | SER372 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 707 |
| Chain | Residue |
| A | HOH1157 |
| A | HOH1314 |
| A | HOH1339 |
| A | HOH1356 |
| A | LYS51 |
| A | TYR55 |
| A | ASN300 |
| A | LEU303 |
| A | HOH1091 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 708 |
| Chain | Residue |
| A | ASN138 |
| A | GLY141 |
| A | GOL701 |
| site_id | BC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE GOL A 709 |
| Chain | Residue |
| A | PRO189 |
| A | THR190 |
| A | LEU191 |
| A | ARG219 |
| A | ASN345 |
| A | HOH1027 |
| A | HOH1049 |
| A | HOH1095 |
| A | HOH1110 |
| A | HOH1193 |
| A | HOH1295 |
| A | HOH1304 |
| A | HOH1363 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 900 |
| Chain | Residue |
| A | GLY220 |
| A | LEU221 |
| A | GLU222 |
| A | GLU223 |
| A | GOL702 |
| A | SO41002 |
| A | HOH1276 |
| A | HOH1280 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 901 |
| Chain | Residue |
| A | GLY41 |
| A | GLY379 |
| A | THR381 |
| A | ASN384 |
| A | HOH1180 |
| A | HOH1182 |
| A | HOH1248 |
| A | HOH1354 |
| site_id | BC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 902 |
| Chain | Residue |
| A | ILE33 |
| A | TYR65 |
| A | KST246 |
| A | ARG280 |
| A | ASN285 |
| A | PSZ600 |
| A | HOH1008 |
| A | HOH1064 |
| A | HOH1218 |
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) |
