eF-site ID 1fdy-ABCD PDB Code 1fdy Chain A, B, C, D click to enlarge Title N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH HYDROXYPYRUVATE Classification LYASE Compound N-ACETYLNEURAMINATE LYASE Source null (NANA_ECOLI) Sequence A:  NLRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLY VGGSTGEAFVQSLSEREQVLEIVAEEGKGKIKLIAHVGCV TTAESQQLAASAKRYGFDAVSAVTPFYYPFSFEEHCDHYR AIIDSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGA LKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGAD GGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVI DLLIKTGVFRGLKTVLHYMDVVSVPLCRKPFGPVDEKYLP ELKALAQQLMQE B:  NLRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLY VGGSTGEAFVQSLSEREQVLEIVAEEGKGKIKLIAHVGCV TTAESQQLAASAKRYGFDAVSAVTPFYYPFSFEEHCDHYR AIIDSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGA LKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGAD GGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVI DLLIKTGVFRGLKTVLHYMDVVSVPLCRKPFGPVDEKYLP ELKALAQQLMQ C:  NLRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLY VGGSTGEAFVQSLSEREQVLEIVAEEGKGKIKLIAHVGCV TTAESQQLAASAKRYGFDAVSAVTPFYYPFSFEEHCDHYR AIIDSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGA LKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGAD GGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVI DLLIKTGVFRGLKTVLHYMDVVSVPLCRKPFGPVDEKYLP ELKALAQQLMQ D:  NLRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLY VGGSTGEAFVQSLSEREQVLEIVAEEGKGKIKLIAHVGCV TTAESQQLAASAKRYGFDAVSAVTPFYYPFSFEEHCDHYR AIIDSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGA LKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGAD GGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVI DLLIKTGVFRGLKTVLHYMDVVSVPLCRKPFGPVDEKYLP ELKALAQQLMQ 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 B residue 11 type sequence A description BINDING SITE FOR RESIDUE 3PY B 804 source : AC2 9) chain B residue 43 type sequence Y description BINDING SITE FOR RESIDUE 3PY B 804 source : AC2 10) chain B residue 46 type sequence G description BINDING SITE FOR RESIDUE 3PY B 804 source : AC2 11) chain B residue 47 type sequence S description BINDING SITE FOR RESIDUE 3PY B 804 source : AC2 12) chain B residue 48 type sequence T description BINDING SITE FOR RESIDUE 3PY B 804 source : AC2 13) chain B residue 137 type sequence Y description BINDING SITE FOR RESIDUE 3PY B 804 source : AC2 14) chain B residue 165 type sequence K description BINDING SITE FOR RESIDUE 3PY B 804 source : AC2 15) chain C residue 43 type sequence Y description BINDING SITE FOR RESIDUE 3PY C 806 source : AC3 16) chain C residue 46 type sequence G description BINDING SITE FOR RESIDUE 3PY C 806 source : AC3 17) chain C residue 47 type sequence S description BINDING SITE FOR RESIDUE 3PY C 806 source : AC3 18) chain C residue 48 type sequence T description BINDING SITE FOR RESIDUE 3PY C 806 source : AC3 19) chain C residue 137 type sequence Y description BINDING SITE FOR RESIDUE 3PY C 806 source : AC3 20) chain C residue 165 type sequence K description BINDING SITE FOR RESIDUE 3PY C 806 source : AC3 21) chain D residue 11 type sequence A description BINDING SITE FOR RESIDUE 3PY D 808 source : AC4 22) chain D residue 43 type sequence Y description BINDING SITE FOR RESIDUE 3PY D 808 source : AC4 23) chain D residue 46 type sequence G description BINDING SITE FOR RESIDUE 3PY D 808 source : AC4 24) chain D residue 47 type sequence S description BINDING SITE FOR RESIDUE 3PY D 808 source : AC4 25) chain D residue 48 type sequence T description BINDING SITE FOR RESIDUE 3PY D 808 source : AC4 26) chain D residue 137 type sequence Y description BINDING SITE FOR RESIDUE 3PY D 808 source : AC4 27) chain D residue 165 type sequence K description BINDING SITE FOR RESIDUE 3PY D 808 source : AC4 28) chain D residue 167 type sequence T description BINDING SITE FOR RESIDUE 3PY D 808 source : AC4 29) chain A residue 138 type catalytic sequence N description 553 source MCSA : MCSA1 30) chain A residue 166 type catalytic sequence Q description 553 source MCSA : MCSA1 31) chain B residue 137 type catalytic sequence Y description 553 source MCSA : MCSA2 32) chain B residue 165 type catalytic sequence K description 553 source MCSA : MCSA2 33) chain C residue 137 type catalytic sequence Y description 553 source MCSA : MCSA3 34) chain C residue 165 type catalytic sequence K description 553 source MCSA : MCSA3 35) chain D residue 137 type catalytic sequence Y description 553 source MCSA : MCSA4 36) chain D residue 165 type catalytic sequence K description 553 source MCSA : MCSA4 37) chain A residue 168 type BINDING sequence S description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 38) chain A residue 190 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 39) chain A residue 192 type BINDING sequence E description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 40) chain A residue 193 type BINDING sequence I description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 41) chain A residue 209 type BINDING sequence T description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 42) chain B residue 167 type BINDING sequence T description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 43) chain B residue 189 type BINDING sequence G description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 44) chain B residue 191 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 45) chain B residue 192 type BINDING sequence E description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 46) chain B residue 208 type BINDING sequence S description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 47) chain C residue 167 type BINDING sequence T description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 48) chain C residue 189 type BINDING sequence G description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 49) chain C residue 191 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 50) chain C residue 192 type BINDING sequence E description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 51) chain C residue 208 type BINDING sequence S description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 52) chain D residue 167 type BINDING sequence T description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 53) chain D residue 189 type BINDING sequence G description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 54) chain D residue 191 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 55) chain D residue 192 type BINDING sequence E description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 56) chain D residue 208 type BINDING sequence S description BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL source Swiss-Prot : SWS_FT_FI4 57) 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 58) 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 59) chain B residue 47 type SITE sequence S description Required to correctly position the proton donor => ECO:0000305|PubMed:24521460 source Swiss-Prot : SWS_FT_FI5 60) chain B residue 110 type SITE sequence Y description Required to correctly position the proton donor => ECO:0000305|PubMed:24521460 source Swiss-Prot : SWS_FT_FI5 61) chain C residue 47 type SITE sequence S description Required to correctly position the proton donor => ECO:0000305|PubMed:24521460 source Swiss-Prot : SWS_FT_FI5 62) chain C residue 110 type SITE sequence Y description Required to correctly position the proton donor => ECO:0000305|PubMed:24521460 source Swiss-Prot : SWS_FT_FI5 63) 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 64) 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 65) 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 66) chain C 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 67) chain B 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 68) 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 69) chain A residue 41-58 type prosite sequence GLYVGGSTGEAFVQSLSE description DHDPS_1 Dihydrodipicolinate synthase signature 1. GLYvgGSTGEAfvqslsE source prosite : PS00665 70) chain A residue 137-167 type prosite sequence YNIPALSGVKLTLDQINTLVTLPGVGALKQT description DHDPS_2 Dihydrodipicolinate synthase signature 2. YNIPalSgvkLtldqintlvtlpg.VgALKQT source prosite : PS00666 71) chain C 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 72) chain C 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 73) 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 74) 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 75) 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 76) chain B 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 77) 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 78) 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 79) chain C residue 137 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:24521460 source Swiss-Prot : SWS_FT_FI1 80) chain A residue 138 type ACT_SITE sequence N description Proton donor => ECO:0000305|PubMed:24521460 source Swiss-Prot : SWS_FT_FI1 81) chain B residue 137 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:24521460 source Swiss-Prot : SWS_FT_FI1 82) 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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