eF-site ID 5vwq-D PDB Code 5vwq Chain D 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 D:  MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDET GKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQE LLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSV KRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFD ALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIV ASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIR ANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR MRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLR LREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL Description Functional site 1) chain D residue 65 type sequence Y description binding site for residue PMP A 401 source : AC1 2) chain D residue 103 type sequence G description binding site for residue PMP D 401 source : AC2 3) chain D residue 104 type sequence T description binding site for residue PMP D 401 source : AC2 4) chain D residue 130 type sequence W description binding site for residue PMP D 401 source : AC2 5) chain D residue 183 type sequence N description binding site for residue PMP D 401 source : AC2 6) chain D residue 211 type sequence D description binding site for residue PMP D 401 source : AC2 7) chain D residue 214 type sequence Y description binding site for residue PMP D 401 source : AC2 8) chain D residue 243 type sequence S description binding site for residue PMP D 401 source : AC2 9) chain D residue 245 type sequence S description binding site for residue PMP D 401 source : AC2 10) chain D residue 246 type sequence K description binding site for residue PMP D 401 source : AC2 11) chain D residue 254 type sequence R description binding site for residue PMP D 401 source : AC2 12) chain D residue 130 type catalytic sequence W description 777 source MCSA : MCSA2 13) chain D residue 211 type catalytic sequence D description 777 source MCSA : MCSA2 14) chain D residue 246 type catalytic sequence K description 777 source MCSA : MCSA2 15) 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 16) 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 17) 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 18) 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 19) 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

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