eF-site ID 1fdy-B PDB Code 1fdy Chain B 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 B:  NLRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLY VGGSTGEAFVQSLSEREQVLEIVAEEGKGKIKLIAHVGCV TTAESQQLAASAKRYGFDAVSAVTPFYYPFSFEEHCDHYR AIIDSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGA LKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGAD GGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVI DLLIKTGVFRGLKTVLHYMDVVSVPLCRKPFGPVDEKYLP ELKALAQQLMQ Description Functional site 1) chain B residue 11 type sequence A description BINDING SITE FOR RESIDUE 3PY B 804 source : AC2 2) chain B residue 43 type sequence Y description BINDING SITE FOR RESIDUE 3PY B 804 source : AC2 3) chain B residue 46 type sequence G description BINDING SITE FOR RESIDUE 3PY B 804 source : AC2 4) chain B residue 47 type sequence S description BINDING SITE FOR RESIDUE 3PY B 804 source : AC2 5) chain B residue 48 type sequence T description BINDING SITE FOR RESIDUE 3PY B 804 source : AC2 6) chain B residue 137 type sequence Y description BINDING SITE FOR RESIDUE 3PY B 804 source : AC2 7) chain B residue 165 type sequence K description BINDING SITE FOR RESIDUE 3PY B 804 source : AC2 8) chain B residue 138 type catalytic sequence N description 553 source MCSA : MCSA2 9) chain B residue 166 type catalytic sequence Q description 553 source MCSA : MCSA2 10) chain B residue 138 type ACT_SITE sequence N description Proton donor => ECO:0000305|PubMed:24521460 source Swiss-Prot : SWS_FT_FI1 11) chain B 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 12) chain B 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 13) chain B 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 14) chain B residue 209 type BINDING sequence T description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 15) chain B residue 168 type BINDING sequence S description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 16) chain B residue 190 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 17) chain B residue 192 type BINDING sequence E description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 18) chain B residue 193 type BINDING sequence I description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 19) chain B residue 48 type SITE sequence T description Required to correctly position the proton donor => ECO:0000305|PubMed:24521460 source Swiss-Prot : SWS_FT_FI5 20) chain B 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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