eF-site ID 1f73-ABCD PDB Code 1f73 Chain A, B, C, D 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 Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) (NANA_HAEIN) Sequence A:  MRDLKGIFSALLVSFNEDGTINEKGLRQIIRHNIDKMKVD GLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQV GSVNLKEAVELGKYATELGYDCLSAVTPFYYKFSFPEIKH YYDTIIAETGSNMIVYSIPNMGIEQFGELYKNPKVLGVKF TAGDFYLLERLKKAYPNHLIWAGFDEMMLPAASLGVDGAI GSTFNVNGVRARQIFELTKAGKLKEALEIQHVTNDLIEGI LANGLYLTIKELLKLEGVDAGYCREPMTSKATAEQVAKAK DLKAKFLS B:  MRDLKGIFSALLVSFNEDGTINEKGLRQIIRHNIDKMKVD GLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQV GSVNLKEAVELGKYATELGYDCLSAVTPFYYKFSFPEIKH YYDTIIAETGSNMIVYSIPNMGIEQFGELYKNPKVLGVKF TAGDFYLLERLKKAYPNHLIWAGFDEMMLPAASLGVDGAI GSTFNVNGVRARQIFELTKAGKLKEALEIQHVTNDLIEGI LANGLYLTIKELLKLEGVDAGYCREPMTSKATAEQVAKAK DLKAKFLS C:  MRDLKGIFSALLVSFNEDGTINEKGLRQIIRHNIDKMKVD GLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQV GSVNLKEAVELGKYATELGYDCLSAVTPFYYKFSFPEIKH YYDTIIAETGSNMIVYSIPNMGIEQFGELYKNPKVLGVKF TAGDFYLLERLKKAYPNHLIWAGFDEMMLPAASLGVDGAI GSTFNVNGVRARQIFELTKAGKLKEALEIQHVTNDLIEGI LANGLYLTIKELLKLEGVDAGYCREPMTSKATAEQVAKAK DLKAKFLS D:  MRDLKGIFSALLVSFNEDGTINEKGLRQIIRHNIDKMKVD GLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQV GSVNLKEAVELGKYATELGYDCLSAVTPFYYKFSFPEIKH YYDTIIAETGSNMIVYSIPNMGIEQFGELYKNPKVLGVKF TAGDFYLLERLKKAYPNHLIWAGFDEMMLPAASLGVDGAI GSTFNVNGVRARQIFELTKAGKLKEALEIQHVTNDLIEGI LANGLYLTIKELLKLEGVDAGYCREPMTSKATAEQVAKAK DLKAKFLS Description Functional site 1) chain A residue 10 type sequence A description BINDING SITE FOR RESIDUE HMN A 700 source : AC1 2) chain A residue 43 type sequence Y description BINDING SITE FOR RESIDUE HMN A 700 source : AC1 3) chain A residue 46 type sequence G description BINDING SITE FOR RESIDUE HMN A 700 source : AC1 4) chain A residue 47 type sequence S description BINDING SITE FOR RESIDUE HMN A 700 source : AC1 5) chain A residue 48 type sequence T description BINDING SITE FOR RESIDUE HMN A 700 source : AC1 6) chain A residue 164 type sequence K description BINDING SITE FOR RESIDUE HMN A 700 source : AC1 7) chain A residue 188 type sequence G description BINDING SITE FOR RESIDUE HMN A 700 source : AC1 8) chain A residue 190 type sequence D description BINDING SITE FOR RESIDUE HMN A 700 source : AC1 9) chain A residue 191 type sequence E description BINDING SITE FOR RESIDUE HMN A 700 source : AC1 10) chain A residue 206 type sequence G description BINDING SITE FOR RESIDUE HMN A 700 source : AC1 11) chain A residue 207 type sequence S description BINDING SITE FOR RESIDUE HMN A 700 source : AC1 12) chain A residue 250 type sequence L description BINDING SITE FOR RESIDUE HMN A 700 source : AC1 13) chain B residue 10 type sequence A description BINDING SITE FOR RESIDUE HMN B 701 source : AC2 14) chain B residue 43 type sequence Y description BINDING SITE FOR RESIDUE HMN B 701 source : AC2 15) chain B residue 46 type sequence G description BINDING SITE FOR RESIDUE HMN B 701 source : AC2 16) chain B residue 47 type sequence S description BINDING SITE FOR RESIDUE HMN B 701 source : AC2 17) chain B residue 48 type sequence T description BINDING SITE FOR RESIDUE HMN B 701 source : AC2 18) chain B residue 164 type sequence K description BINDING SITE FOR RESIDUE HMN B 701 source : AC2 19) chain B residue 188 type sequence G description BINDING SITE FOR RESIDUE HMN B 701 source : AC2 20) chain B residue 190 type sequence D description BINDING SITE FOR RESIDUE HMN B 701 source : AC2 21) chain B residue 191 type sequence E description BINDING SITE FOR RESIDUE HMN B 701 source : AC2 22) chain B residue 206 type sequence G description BINDING SITE FOR RESIDUE HMN B 701 source : AC2 23) chain B residue 207 type sequence S description BINDING SITE FOR RESIDUE HMN B 701 source : AC2 24) chain B residue 250 type sequence L description BINDING SITE FOR RESIDUE HMN B 701 source : AC2 25) chain C residue 10 type sequence A description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 26) chain C residue 43 type sequence Y description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 27) chain C residue 46 type sequence G description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 28) chain C residue 47 type sequence S description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 29) chain C residue 48 type sequence T description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 30) chain C residue 164 type sequence K description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 31) chain C residue 188 type sequence G description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 32) chain C residue 190 type sequence D description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 33) chain C residue 191 type sequence E description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 34) chain C residue 205 type sequence I description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 35) chain C residue 206 type sequence G description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 36) chain C residue 207 type sequence S description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 37) chain C residue 250 type sequence L description BINDING SITE FOR RESIDUE HMN C 702 source : AC3 38) chain D residue 10 type sequence A description BINDING SITE FOR RESIDUE HMN D 703 source : AC4 39) chain D residue 43 type sequence Y description BINDING SITE FOR RESIDUE HMN D 703 source : AC4 40) chain D residue 46 type sequence G description BINDING SITE FOR RESIDUE HMN D 703 source : AC4 41) chain D residue 47 type sequence S description BINDING SITE FOR RESIDUE HMN D 703 source : AC4 42) chain D residue 48 type sequence T description BINDING SITE FOR RESIDUE HMN D 703 source : AC4 43) chain D residue 164 type sequence K description BINDING SITE FOR RESIDUE HMN D 703 source : AC4 44) chain D residue 188 type sequence G description BINDING SITE FOR RESIDUE HMN D 703 source : AC4 45) chain D residue 189 type sequence F description BINDING SITE FOR RESIDUE HMN D 703 source : AC4 46) chain D residue 190 type sequence D description BINDING SITE FOR RESIDUE HMN D 703 source : AC4 47) chain D residue 191 type sequence E description BINDING SITE FOR RESIDUE HMN D 703 source : AC4 48) chain D residue 206 type sequence G description BINDING SITE FOR RESIDUE HMN D 703 source : AC4 49) chain D residue 207 type sequence S description BINDING SITE FOR RESIDUE HMN D 703 source : AC4 50) chain D residue 250 type sequence L description BINDING SITE FOR RESIDUE HMN D 703 source : AC4 51) chain B residue 52 type sequence F description BINDING SITE FOR RESIDUE GOL B 704 source : AC5 52) chain B residue 54 type sequence L description BINDING SITE FOR RESIDUE GOL B 704 source : AC5 53) chain B residue 59 type sequence K description BINDING SITE FOR RESIDUE GOL B 704 source : AC5 54) chain B residue 82 type sequence S description BINDING SITE FOR RESIDUE GOL B 704 source : AC5 55) chain B residue 87 type sequence E description BINDING SITE FOR RESIDUE GOL B 704 source : AC5 56) chain A residue 39-64 type prosite sequence VDGLYVGGSTGENFMLSTEEKKEIFR description SUGAR_TRANSPORT_2 Sugar transport proteins signature 2. VdGLYvGGstgenfmLstEekkeifR source prosite : PS00217 57) chain A residue 1-4 type prosite sequence MRDL description TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MRDL source prosite : PS00228 58) chain A residue 41-58 type prosite sequence GLYVGGSTGENFMLSTEE description DHDPS_1 Dihydrodipicolinate synthase signature 1. GLYvgGSTGENfmlsteE source prosite : PS00665 59) chain A residue 136-166 type prosite sequence YSIPNMGIEQFGELYKNPKVLGVKFT description DHDPS_2 Dihydrodipicolinate synthase signature 2. YSIPflTgvnMgieqfgelyknpk.VlGVKFT source prosite : PS00666 60) chain A residue 47 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 61) chain B residue 166 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 62) chain B residue 188 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 63) chain B residue 190 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 64) chain B residue 191 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 65) chain B residue 207 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 66) chain C residue 47 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 67) chain C residue 48 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 68) chain C residue 166 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 69) chain C residue 188 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 70) chain C residue 190 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 71) chain A residue 48 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 72) chain C residue 191 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 73) chain C residue 207 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 74) chain D residue 47 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 75) chain D residue 48 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 76) chain D residue 166 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 77) chain D residue 188 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 78) chain D residue 190 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 79) chain D residue 191 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 80) chain D residue 207 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 81) chain A residue 166 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 82) chain A residue 188 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 83) chain A residue 190 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 84) chain A residue 191 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 85) chain A residue 207 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 86) chain B residue 47 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 87) chain B residue 48 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_01237 source Swiss-Prot : SWS_FT_FI3 88) chain A 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 89) chain B 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 90) 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 91) chain D 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 92) chain A 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 93) chain B 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 94) 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 95) chain D 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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