eF-site ID 1ahg-A PDB Code 1ahg Chain A click to enlarge Title ASPARTATE AMINOTRANSFERASE HEXAMUTANT Classification TRANSFERASE (AMINOTRANSFERASE) Compound Aspartate aminotransferase Source null (AAT_ECOLI) Sequence A:  MFENITAAPADPILGLADLFRADERPGKINLGIGLYYDET GKIPVLTSVKKAEQYLLENETTKLYLGIDGIPEFGRCTQE LLFGKGSALINDKRARTAQTPGGSGALRVAADFLAKNTSV KRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFD ALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIV ASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIR ANYSSPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR MRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLR LREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL Description Functional site 1) chain A residue 15 type sequence D description source : ACT 2) chain A residue 17 type sequence I description source : ACT 3) chain A residue 18 type sequence L description source : ACT 4) chain A residue 37 type sequence I description source : ACT 5) chain A residue 38 type sequence G description source : ACT 6) chain A residue 39 type sequence L description source : ACT 7) chain A residue 107 type sequence G description source : ACT 8) chain A residue 108 type sequence G description source : ACT 9) chain A residue 109 type sequence S description source : ACT 10) chain A residue 140 type sequence W description source : ACT 11) chain A residue 194 type sequence N description source : ACT 12) chain A residue 222 type sequence D description source : ACT 13) chain A residue 224 type sequence A description source : ACT 14) chain A residue 225 type sequence Y description source : ACT 15) chain A residue 255 type sequence S description source : ACT 16) chain A residue 258 type sequence K description source : ACT 17) chain A residue 266 type sequence R description source : ACT 18) chain A residue 360 type sequence F description source : ACT 19) chain A residue 386 type sequence R description source : ACT 20) chain A residue 70 type sequence Y description source : BCT 21) chain A residue 292 type sequence R description source : BCT 22) chain A residue 296 type sequence S description source : BCT 23) chain A residue 297 type sequence S description source : BCT 24) chain A residue 108 type sequence G description BINDING SITE FOR RESIDUE PLP C 410 source : AC1 25) chain A residue 109 type sequence S description BINDING SITE FOR RESIDUE PLP C 410 source : AC1 26) chain A residue 140 type sequence W description BINDING SITE FOR RESIDUE PLP C 410 source : AC1 27) chain A residue 194 type sequence N description BINDING SITE FOR RESIDUE PLP C 410 source : AC1 28) chain A residue 222 type sequence D description BINDING SITE FOR RESIDUE PLP C 410 source : AC1 29) chain A residue 225 type sequence Y description BINDING SITE FOR RESIDUE PLP C 410 source : AC1 30) chain A residue 255 type sequence S description BINDING SITE FOR RESIDUE PLP C 410 source : AC1 31) chain A residue 257 type sequence S description BINDING SITE FOR RESIDUE PLP C 410 source : AC1 32) chain A residue 266 type sequence R description BINDING SITE FOR RESIDUE PLP C 410 source : AC1 33) chain A residue 70 type sequence Y description BINDING SITE FOR RESIDUE PLP D 410 source : AC2 34) chain A residue 140 type catalytic sequence W description 777 source MCSA : MCSA1 35) chain A residue 222 type catalytic sequence D description 777 source MCSA : MCSA1 36) chain A residue 258 type catalytic sequence K description 777 source MCSA : MCSA1 37) 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 38) 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 39) chain A residue 38 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 40) chain A residue 140 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 41) 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 42) chain A residue 194 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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