eF-site ID 1ahg-B PDB Code 1ahg Chain B click to enlarge Title ASPARTATE AMINOTRANSFERASE HEXAMUTANT Classification TRANSFERASE (AMINOTRANSFERASE) Compound Aspartate aminotransferase Source Escherichia coli (strain K12) (AAT_ECOLI) Sequence B:  MFENITAAPADPILGLADLFRADERPGKINLGIGLYYDET GKIPVLTSVKKAEQYLLENETTKLYLGIDGIPEFGRCTQE LLFGKGSALINDKRARTAQTPGGSGALRVAADFLAKNTSV KRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFD ALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIV ASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIR ANYSSPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR MRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLR LREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL Description Functional site 1) chain B residue 70 type sequence Y description source : ACT 2) chain B residue 292 type sequence R description source : ACT 3) chain B residue 296 type sequence S description source : ACT 4) chain B residue 297 type sequence S description source : ACT 5) chain B residue 15 type sequence D description source : BCT 6) chain B residue 17 type sequence I description source : BCT 7) chain B residue 18 type sequence L description source : BCT 8) chain B residue 37 type sequence I description source : BCT 9) chain B residue 38 type sequence G description source : BCT 10) chain B residue 39 type sequence L description source : BCT 11) chain B residue 107 type sequence G description source : BCT 12) chain B residue 108 type sequence G description source : BCT 13) chain B residue 109 type sequence S description source : BCT 14) chain B residue 140 type sequence W description source : BCT 15) chain B residue 194 type sequence N description source : BCT 16) chain B residue 222 type sequence D description source : BCT 17) chain B residue 224 type sequence A description source : BCT 18) chain B residue 225 type sequence Y description source : BCT 19) chain B residue 255 type sequence S description source : BCT 20) chain B residue 258 type sequence K description source : BCT 21) chain B residue 266 type sequence R description source : BCT 22) chain B residue 360 type sequence F description source : BCT 23) chain B residue 386 type sequence R description source : BCT 24) chain B residue 70 type sequence Y description BINDING SITE FOR RESIDUE PLP C 410 source : AC1 25) chain B residue 108 type sequence G description BINDING SITE FOR RESIDUE PLP D 410 source : AC2 26) chain B residue 109 type sequence S description BINDING SITE FOR RESIDUE PLP D 410 source : AC2 27) chain B residue 140 type sequence W description BINDING SITE FOR RESIDUE PLP D 410 source : AC2 28) chain B residue 194 type sequence N description BINDING SITE FOR RESIDUE PLP D 410 source : AC2 29) chain B residue 222 type sequence D description BINDING SITE FOR RESIDUE PLP D 410 source : AC2 30) chain B residue 225 type sequence Y description BINDING SITE FOR RESIDUE PLP D 410 source : AC2 31) chain B residue 255 type sequence S description BINDING SITE FOR RESIDUE PLP D 410 source : AC2 32) chain B residue 257 type sequence S description BINDING SITE FOR RESIDUE PLP D 410 source : AC2 33) chain B residue 266 type sequence R description BINDING SITE FOR RESIDUE PLP D 410 source : AC2 34) chain B 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 35) chain B 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 36) chain B residue 140 type catalytic sequence W description 777 source MCSA : MCSA2 37) chain B residue 222 type catalytic sequence D description 777 source MCSA : MCSA2 38) chain B residue 258 type catalytic sequence K description 777 source MCSA : MCSA2 39) chain B 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 40) chain B 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 41) chain B 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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