eF-site ID 1fdy-D PDB Code 1fdy Chain D 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 D:  NLRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLY VGGSTGEAFVQSLSEREQVLEIVAEEGKGKIKLIAHVGCV TTAESQQLAASAKRYGFDAVSAVTPFYYPFSFEEHCDHYR AIIDSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGA LKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGAD GGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVI DLLIKTGVFRGLKTVLHYMDVVSVPLCRKPFGPVDEKYLP ELKALAQQLMQ Description Functional site 1) chain D residue 11 type sequence A description BINDING SITE FOR RESIDUE 3PY D 808 source : AC4 2) chain D residue 43 type sequence Y description BINDING SITE FOR RESIDUE 3PY D 808 source : AC4 3) chain D residue 46 type sequence G description BINDING SITE FOR RESIDUE 3PY D 808 source : AC4 4) chain D residue 47 type sequence S description BINDING SITE FOR RESIDUE 3PY D 808 source : AC4 5) chain D residue 48 type sequence T description BINDING SITE FOR RESIDUE 3PY D 808 source : AC4 6) chain D residue 137 type sequence Y description BINDING SITE FOR RESIDUE 3PY D 808 source : AC4 7) chain D residue 165 type sequence K description BINDING SITE FOR RESIDUE 3PY D 808 source : AC4 8) chain D residue 167 type sequence T description BINDING SITE FOR RESIDUE 3PY D 808 source : AC4 9) chain D residue 137 type catalytic sequence Y description 553 source MCSA : MCSA4 10) chain D residue 165 type catalytic sequence K description 553 source MCSA : MCSA4 11) chain D residue 167 type BINDING sequence T description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 12) chain D residue 189 type BINDING sequence G description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 13) chain D residue 191 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 14) chain D residue 192 type BINDING sequence E description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 15) chain D residue 208 type BINDING sequence S description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 16) chain D residue 47 type SITE sequence S description Required to correctly position the proton donor => ECO:0000305|PubMed:24521460 source Swiss-Prot : SWS_FT_FI5 17) chain D residue 110 type SITE sequence Y description Required to correctly position the proton donor => ECO:0000305|PubMed:24521460 source Swiss-Prot : SWS_FT_FI5 18) chain D residue 165 type ACT_SITE sequence K 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 19) chain D residue 47 type BINDING sequence S 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 20) chain D 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 21) chain D residue 137 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:24521460 source Swiss-Prot : SWS_FT_FI1

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