eF-site ID 1f73-C PDB Code 1f73 Chain C click to enlarge Title CRYSTAL STRUCTURE ANALYSIS OF N-ACETYLNEURAMINATE LYASE FROM HAEMOPHILUS INFLUENZAE: CRYSTAL FORM III IN COMPLEX WITH SIALIC ACID ALDITOL Classification LYASE Compound N-ACETYL NEURAMINATE LYASE Source null (NANA_HAEIN) Sequence C:  MRDLKGIFSALLVSFNEDGTINEKGLRQIIRHNIDKMKVD GLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQV GSVNLKEAVELGKYATELGYDCLSAVTPFYYKFSFPEIKH YYDTIIAETGSNMIVYSIPNMGIEQFGELYKNPKVLGVKF TAGDFYLLERLKKAYPNHLIWAGFDEMMLPAASLGVDGAI GSTFNVNGVRARQIFELTKAGKLKEALEIQHVTNDLIEGI LANGLYLTIKELLKLEGVDAGYCREPMTSKATAEQVAKAK DLKAKFLS Description Functional site 1) chain C residue 10 type sequence A description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 2) chain C residue 43 type sequence Y description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 3) chain C residue 46 type sequence G description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 4) chain C residue 47 type sequence S description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 5) chain C residue 48 type sequence T description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 6) chain C residue 164 type sequence K description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 7) chain C residue 188 type sequence G description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 8) chain C residue 190 type sequence D description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 9) chain C residue 191 type sequence E description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 10) chain C residue 205 type sequence I description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 11) chain C residue 206 type sequence G description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 12) chain C residue 207 type sequence S description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 13) chain C residue 250 type sequence L description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 14) chain C residue 47 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 15) chain C residue 48 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 16) chain C residue 166 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 17) chain C residue 188 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 18) chain C residue 190 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 19) chain C residue 191 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 20) chain C residue 207 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 21) chain C residue 136 type ACT_SITE sequence Y description Proton donor => ECO:0000255|HAMAP-Rule:MF_01237, ECO:0000305|PubMed:11031117 source Swiss-Prot : SWS_FT_FI1 22) chain C residue 164 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_01237, ECO:0000305|PubMed:11031117 source Swiss-Prot : SWS_FT_FI2

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