eF-site ID 1asb-A PDB Code 1asb Chain A click to enlarge Title THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE D223A(D222A) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE Classification AMINOTRANSFERASE Compound ASPARTATE AMINOTRANSFERASE Source Escherichia coli (strain K12) (AAT_ECOLI) Sequence A:  MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDET GKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQE LLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSV KRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFD ALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL SVEKGWLPLFAFAYQGFARGLEEDAEGLRAFAAMHKELIV ASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIR ANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR MRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLR LREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL Description (1)  ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) MUTANT WITH ASP 223 REPLACED BY ALA (D223A) AND COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE AND MALEATE Functional site 1) chain A residue 258 type sequence K description source : ACT 2) chain A residue 386 type sequence R description source : ACT 3) chain A residue 292 type sequence R description source : ACT 4) chain A residue 77 type sequence Y description BINDING SITE FOR RESIDUE PLP A 409 source : AC1 5) chain A residue 114 type sequence G description BINDING SITE FOR RESIDUE PLP A 409 source : AC1 6) chain A residue 115 type sequence G description BINDING SITE FOR RESIDUE PLP A 409 source : AC1 7) chain A residue 116 type sequence T description BINDING SITE FOR RESIDUE PLP A 409 source : AC1 8) chain A residue 142 type sequence W description BINDING SITE FOR RESIDUE PLP A 409 source : AC1 9) chain A residue 195 type sequence N description BINDING SITE FOR RESIDUE PLP A 409 source : AC1 10) chain A residue 225 type sequence A description BINDING SITE FOR RESIDUE PLP A 409 source : AC1 11) chain A residue 226 type sequence Y description BINDING SITE FOR RESIDUE PLP A 409 source : AC1 12) chain A residue 255 type sequence S description BINDING SITE FOR RESIDUE PLP A 409 source : AC1 13) chain A residue 257 type sequence S description BINDING SITE FOR RESIDUE PLP A 409 source : AC1 14) chain A residue 258 type sequence K description BINDING SITE FOR RESIDUE PLP A 409 source : AC1 15) chain A residue 266 type sequence R description BINDING SITE FOR RESIDUE PLP A 409 source : AC1 16) chain A residue 25 type sequence I description BINDING SITE FOR RESIDUE MAE A 410 source : AC2 17) chain A residue 45 type sequence I description BINDING SITE FOR RESIDUE MAE A 410 source : AC2 18) chain A residue 46 type sequence G description BINDING SITE FOR RESIDUE MAE A 410 source : AC2 19) chain A residue 142 type sequence W description BINDING SITE FOR RESIDUE MAE A 410 source : AC2 20) chain A residue 195 type sequence N description BINDING SITE FOR RESIDUE MAE A 410 source : AC2 21) chain A residue 258 type sequence K description BINDING SITE FOR RESIDUE MAE A 410 source : AC2 22) chain A residue 292 type sequence R description BINDING SITE FOR RESIDUE MAE A 410 source : AC2 23) chain A residue 386 type sequence R description BINDING SITE FOR RESIDUE MAE A 410 source : AC2 24) chain A residue 46 type BINDING sequence G description BINDING => ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC source Swiss-Prot : SWS_FT_FI1 25) chain A residue 142 type BINDING sequence W description 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 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 142 type catalytic sequence W description 777 source MCSA : MCSA1 27) chain A residue 223 type catalytic sequence A description 777 source MCSA : MCSA1 28) chain A residue 258 type catalytic sequence K description 777 source MCSA : MCSA1 29) chain A residue 386 type BINDING sequence R description 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 source Swiss-Prot : SWS_FT_FI4 30) chain A residue 258 type MOD_RES sequence K description 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 source Swiss-Prot : SWS_FT_FI5 31) chain A residue 255-268 type prosite sequence SYSKNFGLYNERVG description AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SYSKnfGLyNERVG source prosite : PS00105 32) chain A residue 195 type BINDING sequence N description 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 source Swiss-Prot : SWS_FT_FI3

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