eF-site ID 1fdy-A PDB Code 1fdy Chain A click to enlarge Title N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH HYDROXYPYRUVATE Classification LYASE Compound N-ACETYLNEURAMINATE LYASE Source Escherichia coli (strain K12) (NANA_ECOLI) Sequence A:  NLRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLY VGGSTGEAFVQSLSEREQVLEIVAEEGKGKIKLIAHVGCV TTAESQQLAASAKRYGFDAVSAVTPFYYPFSFEEHCDHYR AIIDSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGA LKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGAD GGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVI DLLIKTGVFRGLKTVLHYMDVVSVPLCRKPFGPVDEKYLP ELKALAQQLMQE Description Functional site 1) chain A residue 11 type sequence A description BINDING SITE FOR RESIDUE 3PY A 802 source : AC1 2) chain A residue 43 type sequence Y description BINDING SITE FOR RESIDUE 3PY A 802 source : AC1 3) chain A residue 46 type sequence G description BINDING SITE FOR RESIDUE 3PY A 802 source : AC1 4) chain A residue 47 type sequence S description BINDING SITE FOR RESIDUE 3PY A 802 source : AC1 5) chain A residue 48 type sequence T description BINDING SITE FOR RESIDUE 3PY A 802 source : AC1 6) chain A residue 137 type sequence Y description BINDING SITE FOR RESIDUE 3PY A 802 source : AC1 7) chain A residue 165 type sequence K description BINDING SITE FOR RESIDUE 3PY A 802 source : AC1 8) chain A residue 138 type catalytic sequence N description 553 source MCSA : MCSA1 9) chain A residue 166 type catalytic sequence Q description 553 source MCSA : MCSA1 10) chain A residue 41-58 type prosite sequence GLYVGGSTGEAFVQSLSE description DHDPS_1 Dihydrodipicolinate synthase signature 1. GLYvgGSTGEAfvqslsE source prosite : PS00665 11) chain A residue 137-167 type prosite sequence YNIPALSGVKLTLDQINTLVTLPGVGALKQT description DHDPS_2 Dihydrodipicolinate synthase signature 2. YNIPalSgvkLtldqintlvtlpg.VgALKQT source prosite : PS00666 12) chain A residue 138 type ACT_SITE sequence N description Proton donor => ECO:0000305|PubMed:24521460 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 166 type ACT_SITE sequence Q description Schiff-base intermediate with substrate => ECO:0000269|PubMed:12711733, ECO:0000269|PubMed:19923724, ECO:0000269|PubMed:24521460, ECO:0000269|PubMed:9047371, ECO:0000305|PubMed:8081752 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 48 type BINDING sequence T description BINDING => ECO:0000269|PubMed:9047371, ECO:0000305|PubMed:12711733, ECO:0007744|PDB:1FDY, ECO:0007744|PDB:1FDZ, ECO:0007744|PDB:1HL2 source Swiss-Prot : SWS_FT_FI3 15) chain A residue 49 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9047371, ECO:0000305|PubMed:12711733, ECO:0007744|PDB:1FDY, ECO:0007744|PDB:1FDZ, ECO:0007744|PDB:1HL2 source Swiss-Prot : SWS_FT_FI3 16) chain A residue 168 type BINDING sequence S description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 17) chain A residue 190 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 18) chain A residue 192 type BINDING sequence E description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 19) chain A residue 193 type BINDING sequence I description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 20) chain A residue 209 type BINDING sequence T description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 21) chain A residue 48 type SITE sequence T description Required to correctly position the proton donor => ECO:0000305|PubMed:24521460 source Swiss-Prot : SWS_FT_FI5 22) chain A residue 111 type SITE sequence Y description Required to correctly position the proton donor => ECO:0000305|PubMed:24521460 source Swiss-Prot : SWS_FT_FI5

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