eF-site ID 5upf-AB PDB Code 5upf Chain A, B click to enlarge Title Crystal structure of human NAMPT with isoindoline urea inhibitor compound 53 Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound Nicotinamide phosphoribosyltransferase Source null (NAMPT_HUMAN) Sequence A:  FNILLATDSYKVTHYKQYPPNTSKVYSYFECREYEETVFY GLQYILNKYLKGKVVTKEKIQEAKDVYKEHFQDDVFNEKG WNYILEKYDGHLPIEIKAVPEGFVIPRGNVLFTVENTDPE CYWLTNWIETILVQSWYPITVATNSREQKKILAKYLLETS GNLDGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDT VAGLALIKKYYGTKDPVPGYSVPAAEHSTITAWGKDHEKD AFEHIVTQFSSVPVSVVSDSYDIYNACEKIWGEDLRHLIV SRSTQAPLIIRPDSGNPLDTVLKVLEILGKKFPVTENSKG YKLLPPYLRVIQGDGVDINTLQEIVEGMKQKMWSIENIAF GSGGGLLQKLTRDLLNCSFKCSYVVTNGLGINVFKDPVAD PNKRSKKGRLSLHRTPAGNFVTLEEGKGDLEEYGQDLLHT VFKNGKVTKSYSFDEIRKNAQLNI B:  FNILLATDSYKVTHYKQYPPNTSKVYSYFECREYEETVFY GLQYILNKYLKGKVVTKEKIQEAKDVYKEHFQDDVFNEKG WNYILEKYDGHLPIEIKAVPEGFVIPRGNVLFTVENTDPE CYWLTNWIETILVQSWYPITVATNSREQKKILAKYLLETS GNLDGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDT VAGLALIKKYYGTKDPVPGYSVPAAEHSTITAWGKDHEKD AFEHIVTQFSSVPVSVVSDSYDIYNACEKIWGEDLRHLIV SRSTQAPLIIRPDSGNPLDTVLKVLEILGKKFPVTENSKG YKLLPPYLRVIQGDGVDINTLQEIVEGMKQKMWSIENIAF GSGGGLLQKLTRDLLNCSFKCSYVVTNGLGINVFKDPVAD PNKRSKKGRLSLHRTPAGNFVTLEEGKGDLEEYGQDLLHT VFKNGKVTKSYSFDEIRKNAQLNI Description Functional site 1) chain A residue 188 type sequence Y description binding site for residue 8HV A 901 source : AC1 2) chain A residue 189 type sequence K description binding site for residue 8HV A 901 source : AC1 3) chain A residue 191 type sequence H description binding site for residue 8HV A 901 source : AC1 4) chain A residue 193 type sequence F description binding site for residue 8HV A 901 source : AC1 5) chain A residue 196 type sequence R description binding site for residue 8HV A 901 source : AC1 6) chain A residue 219 type sequence D description binding site for residue 8HV A 901 source : AC1 7) chain A residue 244 type sequence A description binding site for residue 8HV A 901 source : AC1 8) chain A residue 275 type sequence S description binding site for residue 8HV A 901 source : AC1 9) chain A residue 309 type sequence I description binding site for residue 8HV A 901 source : AC1 10) chain A residue 311 type sequence R description binding site for residue 8HV A 901 source : AC1 11) chain A residue 349 type sequence R description binding site for residue 8HV A 901 source : AC1 12) chain A residue 351 type sequence I description binding site for residue 8HV A 901 source : AC1 13) chain A residue 379 type sequence A description binding site for residue 8HV A 901 source : AC1 14) chain B residue 18 type sequence Y description binding site for residue 8HV A 901 source : AC1 15) chain A residue 18 type sequence Y description binding site for residue 8HV B 501 source : AC2 16) chain B residue 188 type sequence Y description binding site for residue 8HV B 501 source : AC2 17) chain B residue 189 type sequence K description binding site for residue 8HV B 501 source : AC2 18) chain B residue 191 type sequence H description binding site for residue 8HV B 501 source : AC2 19) chain B residue 193 type sequence F description binding site for residue 8HV B 501 source : AC2 20) chain B residue 196 type sequence R description binding site for residue 8HV B 501 source : AC2 21) chain B residue 219 type sequence D description binding site for residue 8HV B 501 source : AC2 22) chain B residue 244 type sequence A description binding site for residue 8HV B 501 source : AC2 23) chain B residue 275 type sequence S description binding site for residue 8HV B 501 source : AC2 24) chain B residue 311 type sequence R description binding site for residue 8HV B 501 source : AC2 25) chain B residue 349 type sequence R description binding site for residue 8HV B 501 source : AC2 26) chain B residue 351 type sequence I description binding site for residue 8HV B 501 source : AC2 27) chain B residue 379 type sequence A description binding site for residue 8HV B 501 source : AC2 28) chain B residue 247 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 29) chain B residue 311 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 30) chain B residue 353 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI1 31) chain B residue 384 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI1 32) chain B residue 392 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 33) chain A residue 392 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 34) chain B residue 196 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 35) chain B residue 219 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 36) chain A residue 311 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 37) chain A residue 353 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI1 38) chain A residue 384 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI1 39) chain A residue 196 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 40) chain A residue 219 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 41) chain A residue 247 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 42) chain A residue 188 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI3 43) chain B residue 188 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI3 44) chain A residue 472 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 45) chain B residue 472 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4

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