eF-site ID 2gvj-AB PDB Code 2gvj Chain A, B click to enlarge Title Crystal Structure of Human NMPRTase in complex with FK866 Classification TRANSFERASE Compound Nicotinamide phosphoribosyltransferase Source null (NAMPT_HUMAN) Sequence A:  FNILLATDSYKVTHYKQYPPNTSKVYSYFECREYEETVFY GLQYILNKYLKGKVVTKEKIQEAKDVYKEHFQDDVFNEKG WNYILEKYDGHLPIEIKAVPEGFVIPRGNVLFTVENTDPE CYWLTNWIETILVQSWYPITVATNSREQKKILAKYLLETS GNLDGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDT VAGLALIKKYYGTKDPVPGYSVPAAEHSTITAWGKDHEKD AFEHIVTQFSSVPVSVVSDSYDIYNACEKIWGEDLRHLIV SRSTQAPLIIRPDSGNPLDTVLKVLEILGKKFPVTENSKG YKLLPPYLRVIQGDGVDINTLQEIVEGXKQKXWSIENIAF GSGGGLLQKLTRDLLNCSFKCSYVVTNGLGINVFKDPVAD PNKRSKKGRLSLHRTPAGNFVTLEEGKGDLEEYGQDLLHT VFKNGKVTKSYSFDEIRKNAQLNIE B:  FNILLATDSYKVTHYKQYPPNTSKVYSYFECREYEETVFY GLQYILNKYLKGKVVTKEKIQEAKDVYKEHFQDDVFNEKG WNYILEKYDGHLPIEIKAVPEGFVIPRGNVLFTVENTDPE CYWLTNWIETILVQSWYPITVATNSREQKKILAKYLLETS GNLDGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDT VAGLALIKKYYGTKDPVPGYSVPAAEHSTITAWGKDHEKD AFEHIVTQFSSVPVSVVSDSYDIYNACEKIWGEDLRHLIV SRSTQAPLIIRPDSGNPLDTVLKVLEILGKKFPVTENSKG YKLLPPYLRVIQGDGVDINTLQEIVEGXKQKXWSIENIAF GSGGGLLQKLTRDLLNCSFKCSYVVTNGLGINVFKDPVAD PNKRSKKGRLSLHRTPAGNFVTLEEGKGDLEEYGQDLLHT VFKNGKVTKSYSFDEIRKNAQLNI Description (1)  Nicotinamide phosphoribosyltransferase (E.C.2.4.2.12) Functional site 1) chain A residue 18 type sequence Y description BINDING SITE FOR RESIDUE DGB B 501 source : AC1 2) chain B residue 189 type sequence K description BINDING SITE FOR RESIDUE DGB B 501 source : AC1 3) chain B residue 193 type sequence F description BINDING SITE FOR RESIDUE DGB B 501 source : AC1 4) chain B residue 196 type sequence R description BINDING SITE FOR RESIDUE DGB B 501 source : AC1 5) chain B residue 219 type sequence D description BINDING SITE FOR RESIDUE DGB B 501 source : AC1 6) chain B residue 242 type sequence V description BINDING SITE FOR RESIDUE DGB B 501 source : AC1 7) chain B residue 244 type sequence A description BINDING SITE FOR RESIDUE DGB B 501 source : AC1 8) chain B residue 275 type sequence S description BINDING SITE FOR RESIDUE DGB B 501 source : AC1 9) chain B residue 307 type sequence P description BINDING SITE FOR RESIDUE DGB B 501 source : AC1 10) chain B residue 311 type sequence R description BINDING SITE FOR RESIDUE DGB B 501 source : AC1 11) chain B residue 349 type sequence R description BINDING SITE FOR RESIDUE DGB B 501 source : AC1 12) chain B residue 350 type sequence V description BINDING SITE FOR RESIDUE DGB B 501 source : AC1 13) chain B residue 376 type sequence E description BINDING SITE FOR RESIDUE DGB B 501 source : AC1 14) chain B residue 378 type sequence I description BINDING SITE FOR RESIDUE DGB B 501 source : AC1 15) chain B residue 379 type sequence A description BINDING SITE FOR RESIDUE DGB B 501 source : AC1 16) chain A residue 189 type sequence K description BINDING SITE FOR RESIDUE DGB A 502 source : AC2 17) chain A residue 191 type sequence H description BINDING SITE FOR RESIDUE DGB A 502 source : AC2 18) chain A residue 193 type sequence F description BINDING SITE FOR RESIDUE DGB A 502 source : AC2 19) chain A residue 196 type sequence R description BINDING SITE FOR RESIDUE DGB A 502 source : AC2 20) chain A residue 219 type sequence D description BINDING SITE FOR RESIDUE DGB A 502 source : AC2 21) chain A residue 242 type sequence V description BINDING SITE FOR RESIDUE DGB A 502 source : AC2 22) chain A residue 244 type sequence A description BINDING SITE FOR RESIDUE DGB A 502 source : AC2 23) chain A residue 275 type sequence S description BINDING SITE FOR RESIDUE DGB A 502 source : AC2 24) chain A residue 307 type sequence P description BINDING SITE FOR RESIDUE DGB A 502 source : AC2 25) chain A residue 311 type sequence R description BINDING SITE FOR RESIDUE DGB A 502 source : AC2 26) chain A residue 349 type sequence R description BINDING SITE FOR RESIDUE DGB A 502 source : AC2 27) chain A residue 350 type sequence V description BINDING SITE FOR RESIDUE DGB A 502 source : AC2 28) chain A residue 376 type sequence E description BINDING SITE FOR RESIDUE DGB A 502 source : AC2 29) chain A residue 378 type sequence I description BINDING SITE FOR RESIDUE DGB A 502 source : AC2 30) chain A residue 379 type sequence A description BINDING SITE FOR RESIDUE DGB A 502 source : AC2 31) chain B residue 18 type sequence Y description BINDING SITE FOR RESIDUE DGB A 502 source : AC2 32) chain A residue 472 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 33) chain B residue 472 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 34) chain A residue 311 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 35) chain A residue 353 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI1 36) chain A residue 384 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI1 37) chain B residue 247 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 38) chain B residue 311 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 39) chain B residue 353 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI1 40) chain B residue 384 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI1 41) chain B residue 392 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 42) chain A residue 392 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 43) chain B residue 196 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 44) chain B residue 219 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 45) chain A residue 196 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 46) chain A residue 219 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 47) chain A residue 247 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 48) chain A residue 188 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI3 49) chain B residue 188 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI3

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