eF-site ID 5vwq-ADGJ PDB Code 5vwq Chain A, D, G, J click to enlarge Title E.coli Aspartate aminotransferase-(1R,3S,4S)-3-amino-4-fluorocyclopentane-1-carboxylic acid (FCP) Classification TRANSFERASE Compound Aspartate aminotransferase Source Escherichia coli (strain K12) (AAT_ECOLI) Sequence A:  MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDET GKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQE LLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSV KRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFD ALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIV ASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIR ANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR MRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLR LREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL D:  MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDET GKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQE LLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSV KRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFD ALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIV ASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIR ANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR MRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLR LREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL G:  MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDET GKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQE LLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSV KRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFD ALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIV ASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIR ANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR MRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLR LREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL J:  MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDET GKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQE LLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSV KRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFD ALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIV ASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIR ANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR MRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLR LREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL Description Functional site 1) chain A residue 103 type sequence G description binding site for residue PMP A 401 source : AC1 2) chain A residue 104 type sequence T description binding site for residue PMP A 401 source : AC1 3) chain A residue 130 type sequence W description binding site for residue PMP A 401 source : AC1 4) chain A residue 183 type sequence N description binding site for residue PMP A 401 source : AC1 5) chain A residue 211 type sequence D description binding site for residue PMP A 401 source : AC1 6) chain A residue 214 type sequence Y description binding site for residue PMP A 401 source : AC1 7) chain A residue 243 type sequence S description binding site for residue PMP A 401 source : AC1 8) chain A residue 245 type sequence S description binding site for residue PMP A 401 source : AC1 9) chain A residue 246 type sequence K description binding site for residue PMP A 401 source : AC1 10) chain A residue 254 type sequence R description binding site for residue PMP A 401 source : AC1 11) chain D residue 65 type sequence Y description binding site for residue PMP A 401 source : AC1 12) chain A residue 65 type sequence Y description binding site for residue PMP D 401 source : AC2 13) chain D residue 103 type sequence G description binding site for residue PMP D 401 source : AC2 14) chain D residue 104 type sequence T description binding site for residue PMP D 401 source : AC2 15) chain D residue 130 type sequence W description binding site for residue PMP D 401 source : AC2 16) chain D residue 183 type sequence N description binding site for residue PMP D 401 source : AC2 17) chain D residue 211 type sequence D description binding site for residue PMP D 401 source : AC2 18) chain D residue 214 type sequence Y description binding site for residue PMP D 401 source : AC2 19) chain D residue 243 type sequence S description binding site for residue PMP D 401 source : AC2 20) chain D residue 245 type sequence S description binding site for residue PMP D 401 source : AC2 21) chain D residue 246 type sequence K description binding site for residue PMP D 401 source : AC2 22) chain D residue 254 type sequence R description binding site for residue PMP D 401 source : AC2 23) chain G residue 102 type sequence G description binding site for residue PMP G 401 source : AC3 24) chain G residue 103 type sequence G description binding site for residue PMP G 401 source : AC3 25) chain G residue 104 type sequence T description binding site for residue PMP G 401 source : AC3 26) chain G residue 130 type sequence W description binding site for residue PMP G 401 source : AC3 27) chain G residue 183 type sequence N description binding site for residue PMP G 401 source : AC3 28) chain G residue 211 type sequence D description binding site for residue PMP G 401 source : AC3 29) chain G residue 214 type sequence Y description binding site for residue PMP G 401 source : AC3 30) chain G residue 243 type sequence S description binding site for residue PMP G 401 source : AC3 31) chain G residue 245 type sequence S description binding site for residue PMP G 401 source : AC3 32) chain G residue 246 type sequence K description binding site for residue PMP G 401 source : AC3 33) chain G residue 254 type sequence R description binding site for residue PMP G 401 source : AC3 34) chain J residue 65 type sequence Y description binding site for residue PMP G 401 source : AC3 35) chain G residue 65 type sequence Y description binding site for residue PMP J 401 source : AC4 36) chain J residue 102 type sequence G description binding site for residue PMP J 401 source : AC4 37) chain J residue 103 type sequence G description binding site for residue PMP J 401 source : AC4 38) chain J residue 104 type sequence T description binding site for residue PMP J 401 source : AC4 39) chain J residue 130 type sequence W description binding site for residue PMP J 401 source : AC4 40) chain J residue 183 type sequence N description binding site for residue PMP J 401 source : AC4 41) chain J residue 211 type sequence D description binding site for residue PMP J 401 source : AC4 42) chain J residue 214 type sequence Y description binding site for residue PMP J 401 source : AC4 43) chain J residue 243 type sequence S description binding site for residue PMP J 401 source : AC4 44) chain J residue 245 type sequence S description binding site for residue PMP J 401 source : AC4 45) chain J residue 246 type sequence K description binding site for residue PMP J 401 source : AC4 46) chain J residue 254 type sequence R description binding site for residue PMP J 401 source : AC4 47) chain A residue 130 type catalytic sequence W description 777 source MCSA : MCSA1 48) chain A residue 211 type catalytic sequence D description 777 source MCSA : MCSA1 49) chain A residue 246 type catalytic sequence K description 777 source MCSA : MCSA1 50) chain D residue 130 type catalytic sequence W description 777 source MCSA : MCSA2 51) chain D residue 211 type catalytic sequence D description 777 source MCSA : MCSA2 52) chain D residue 246 type catalytic sequence K description 777 source MCSA : MCSA2 53) chain G residue 130 type catalytic sequence W description 777 source MCSA : MCSA3 54) chain G residue 211 type catalytic sequence D description 777 source MCSA : MCSA3 55) chain G residue 246 type catalytic sequence K description 777 source MCSA : MCSA3 56) chain J residue 130 type catalytic sequence W description 777 source MCSA : MCSA4 57) chain J residue 211 type catalytic sequence D description 777 source MCSA : MCSA4 58) chain J residue 246 type catalytic sequence K description 777 source MCSA : MCSA4 59) chain A residue 243-256 type prosite sequence SYSKNFGLYNERVG description AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SYSKnfGLyNERVG source prosite : PS00105 60) chain A residue 34 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 61) chain D residue 34 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 62) chain G residue 34 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 63) chain J residue 34 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 64) chain A residue 130 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 65) chain D residue 130 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 66) chain G residue 130 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 67) chain J residue 130 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 68) chain A residue 183 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 69) chain D residue 183 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 70) chain G residue 183 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 71) chain J residue 183 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 72) chain A residue 374 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 73) chain D residue 374 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 74) chain G residue 374 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 75) chain J residue 374 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 76) chain A residue 246 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 77) chain D residue 246 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 78) chain G residue 246 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 79) chain J residue 246 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

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