eF-site ID 1iny-A PDB Code 1iny Chain A click to enlarge Title A SIALIC ACID DERIVED PHOSPHONATE ANALOG INHIBITS DIFFERENT STRAINS OF INFLUENZA VIRUS NEURAMINIDASE WITH DIFFERENT EFFICIENCIES Classification HYDROLASE Compound INFLUENZA A SUBTYPE N9 NEURAMINIDASE Source Influenza A virus (strain A/Tern/Australia/G70C/1975 H11N9) (NRAM_IATRA) Sequence A:  RDFNNLTKGLCTINSWHIYGKDNAVRIGEDSDVLVTREPY VSCDPDECRFYALSQGTTIRGKHSNGTIHDRSQYRALISW PLSSPPTVYNSRVECIGWSSTSCHDGKTRMSICISGPNNN ASAVIWYNRRPVTEINTWARNILRTQESECVCHNGVCPVV FTDGSATGPAETRIYYFKEGKILKWEPLAGTAKHIEECSC YGERAEITCTCRDNWQGSNRPVIRIDPVAMTHTSQYICSP VLTDNPRPNDPTVGKCNDPYPGNNNNGVKGFSYLDGVNTW LGRTISIALRSGYEMLKVPNALTDDKSKPTQGQTIVLNTD WSGYSGSFMDYWAEGECYRACFYVELIRGRPKEDKVWWTS NSIVSMCSSTEFLGQWDWPDGAKIEYFL Description (1)  INFLUENZA A SUBTYPE N9 NEURAMINIDASE (SIALIDASE) (E.C.3.2.1.18) COMPLEXED WITH EPANA INHIBITOR (4-ACETAMIDO-2,4-DIDEOXY-D-GLYCERO-ALPHA-D-GALACTO-1-OCTOPYRANOSYL) PHOSPHONIC ACID Functional site 1) chain A residue 118 type sequence R description SUBSTRATE (SIALIC ACID) BINDING RESIDUES IN CATALYTIC SITE source : CAT 2) chain A residue 119 type sequence E description SUBSTRATE (SIALIC ACID) BINDING RESIDUES IN CATALYTIC SITE source : CAT 3) chain A residue 151 type sequence D description SUBSTRATE (SIALIC ACID) BINDING RESIDUES IN CATALYTIC SITE source : CAT 4) chain A residue 152 type sequence R description SUBSTRATE (SIALIC ACID) BINDING RESIDUES IN CATALYTIC SITE source : CAT 5) chain A residue 179 type sequence W description SUBSTRATE (SIALIC ACID) BINDING RESIDUES IN CATALYTIC SITE source : CAT 6) chain A residue 223 type sequence I description SUBSTRATE (SIALIC ACID) BINDING RESIDUES IN CATALYTIC SITE source : CAT 7) chain A residue 225 type sequence R description SUBSTRATE (SIALIC ACID) BINDING RESIDUES IN CATALYTIC SITE source : CAT 8) chain A residue 277 type sequence E description SUBSTRATE (SIALIC ACID) BINDING RESIDUES IN CATALYTIC SITE source : CAT 9) chain A residue 293 type sequence R description SUBSTRATE (SIALIC ACID) BINDING RESIDUES IN CATALYTIC SITE source : CAT 10) chain A residue 371 type sequence R description SUBSTRATE (SIALIC ACID) BINDING RESIDUES IN CATALYTIC SITE source : CAT 11) chain A residue 405 type sequence Y description SUBSTRATE (SIALIC ACID) BINDING RESIDUES IN CATALYTIC SITE source : CAT 12) chain A residue 151 type catalytic sequence D description 828 source MCSA : MCSA1 13) chain A residue 278 type catalytic sequence E description 828 source MCSA : MCSA1 14) chain A residue 293 type catalytic sequence R description 828 source MCSA : MCSA1 15) chain A residue 371 type catalytic sequence R description 828 source MCSA : MCSA1 16) chain A residue 405 type catalytic sequence Y description 828 source MCSA : MCSA1 17) chain A residue 118 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_04071 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 152 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_04071 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 277 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_04071 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 293 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_04071 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 371 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_04071 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 294 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872, ECO:0000269|PubMed:8371267, ECO:0000269|PubMed:9342319 source Swiss-Prot : SWS_FT_FI4 23) chain A residue 298 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872, ECO:0000269|PubMed:8371267, ECO:0000269|PubMed:9342319 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 325 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872, ECO:0000269|PubMed:8371267, ECO:0000269|PubMed:9342319 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 347 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872, ECO:0000269|PubMed:8371267, ECO:0000269|PubMed:9342319 source Swiss-Prot : SWS_FT_FI4 26) chain A residue 86 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872, ECO:0000269|PubMed:9342319 source Swiss-Prot : SWS_FT_FI5 27) chain A residue 146 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872, ECO:0000269|PubMed:9342319 source Swiss-Prot : SWS_FT_FI5 28) chain A residue 201 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872, ECO:0000269|PubMed:9342319 source Swiss-Prot : SWS_FT_FI5 29) chain A residue 151 type ACT_SITE sequence D description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04071 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 405 type ACT_SITE sequence Y description Nucleophile => ECO:0000255|HAMAP-Rule:MF_04071 source Swiss-Prot : SWS_FT_FI2

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