eF-site ID 1gg5-AC PDB Code 1gg5 Chain A, C click to enlarge Title CRYSTAL STRUCTURE OF A COMPLEX OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE AND A CHEMOTHERAPEUTIC DRUG (E09) AT 2.5 A RESOLUTION Classification OXIDOREDUCTASE Compound NAD(P)H DEHYDROGENASE [QUINONE] 1 Source Homo sapiens (Human) (NQO1_HUMAN) Sequence A:  VGRRALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESD LYAMNFNPIISRKDITGKLKDPANFQYPAESVLAYKEGHL SPDIVAEQKKLEAADLVIFQFPLQWFGVPAILKGWFERVF IGEFAYTYAAMYDKGPFRSKKAVLSITTGGSGSMYSLQGI HGDMNVILWPIQSGILHFCGFQVLEPQLTYSIGHTPADAR IQILEGWKKRLENIWDETPLYFAPSSLFDLNFQAGFLMKK EVQDEEKNKKFGLSVGHHLGKSIPTDNQIKARK C:  VGRRALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESD LYAMNFNPIISRKDITGKLKDPANFQYPAESVLAYKEGHL SPDIVAEQKKLEAADLVIFQFPLQWFGVPAILKGWFERVF IGEFAYTYAAMYDKGPFRSKKAVLSITTGGSGSMYSLQGI HGDMNVILWPIQSGILHFCGFQVLEPQLTYSIGHTPADAR IQILEGWKKRLENIWDETPLYFAPSSLFDLNFQAGFLMKK EVQDEEKNKKFGLSVGHHLGKSIPTDNQIKARK Description Functional site 1) chain A residue 11 type sequence H description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 2) chain A residue 15 type sequence T description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 3) chain A residue 16 type sequence S description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 4) chain A residue 17 type sequence F description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 5) chain A residue 18 type sequence N description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 6) chain A residue 20 type sequence A description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 7) chain A residue 102 type sequence P description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 8) chain A residue 103 type sequence L description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 9) chain A residue 104 type sequence Q description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 10) chain A residue 105 type sequence W description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 11) chain A residue 106 type sequence F description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 12) chain A residue 147 type sequence T description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 13) chain A residue 148 type sequence T description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 14) chain A residue 149 type sequence G description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 15) chain A residue 150 type sequence G description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 16) chain A residue 155 type sequence Y description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 17) chain A residue 192 type sequence I description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 18) chain A residue 200 type sequence R description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 19) chain A residue 204 type sequence L description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 20) chain C residue 66 type sequence Q description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 21) chain C residue 67 type sequence Y description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 22) chain A residue 66 type sequence Q description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 23) chain A residue 67 type sequence Y description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 24) chain C residue 11 type sequence H description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 25) chain C residue 15 type sequence T description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 26) chain C residue 16 type sequence S description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 27) chain C residue 17 type sequence F description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 28) chain C residue 18 type sequence N description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 29) chain C residue 20 type sequence A description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 30) chain C residue 102 type sequence P description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 31) chain C residue 103 type sequence L description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 32) chain C residue 104 type sequence Q description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 33) chain C residue 105 type sequence W description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 34) chain C residue 106 type sequence F description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 35) chain C residue 147 type sequence T description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 36) chain C residue 148 type sequence T description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 37) chain C residue 149 type sequence G description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 38) chain C residue 150 type sequence G description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 39) chain C residue 155 type sequence Y description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 40) chain C residue 192 type sequence I description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 41) chain C residue 200 type sequence R description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 42) chain A residue 105 type sequence W description BINDING SITE FOR RESIDUE E09 C 701 source : AC5 43) chain A residue 106 type sequence F description BINDING SITE FOR RESIDUE E09 C 701 source : AC5 44) chain A residue 149 type sequence G description BINDING SITE FOR RESIDUE E09 C 701 source : AC5 45) chain A residue 150 type sequence G description BINDING SITE FOR RESIDUE E09 C 701 source : AC5 46) chain A residue 161 type sequence H description BINDING SITE FOR RESIDUE E09 C 701 source : AC5 47) chain C residue 68 type sequence P description BINDING SITE FOR RESIDUE E09 C 701 source : AC5 48) chain C residue 126 type sequence Y description BINDING SITE FOR RESIDUE E09 C 701 source : AC5 49) chain C residue 128 type sequence Y description BINDING SITE FOR RESIDUE E09 C 701 source : AC5 50) chain C residue 174 type sequence G description BINDING SITE FOR RESIDUE E09 C 701 source : AC5 51) chain C residue 178 type sequence F description BINDING SITE FOR RESIDUE E09 C 701 source : AC5 52) chain A residue 68 type sequence P description BINDING SITE FOR RESIDUE E09 A 703 source : AC7 53) chain A residue 126 type sequence Y description BINDING SITE FOR RESIDUE E09 A 703 source : AC7 54) chain A residue 128 type sequence Y description BINDING SITE FOR RESIDUE E09 A 703 source : AC7 55) chain A residue 174 type sequence G description BINDING SITE FOR RESIDUE E09 A 703 source : AC7 56) chain A residue 178 type sequence F description BINDING SITE FOR RESIDUE E09 A 703 source : AC7 57) chain C residue 106 type sequence F description BINDING SITE FOR RESIDUE E09 A 703 source : AC7 58) chain C residue 149 type sequence G description BINDING SITE FOR RESIDUE E09 A 703 source : AC7 59) chain C residue 150 type sequence G description BINDING SITE FOR RESIDUE E09 A 703 source : AC7 60) chain C residue 161 type sequence H description BINDING SITE FOR RESIDUE E09 A 703 source : AC7 61) chain A residue 149 type catalytic sequence G description 3 source MCSA : MCSA1 62) chain A residue 155 type catalytic sequence Y description 3 source MCSA : MCSA1 63) chain A residue 161 type catalytic sequence H description 3 source MCSA : MCSA1 64) chain C residue 149 type catalytic sequence G description 3 source MCSA : MCSA3 65) chain C residue 155 type catalytic sequence Y description 3 source MCSA : MCSA3 66) chain C residue 161 type catalytic sequence H description 3 source MCSA : MCSA3 67) chain A residue 11 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396 source Swiss-Prot : SWS_FT_FI1 68) chain C residue 11 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396 source Swiss-Prot : SWS_FT_FI1 69) chain C residue 17 type BINDING sequence F description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396 source Swiss-Prot : SWS_FT_FI1 70) chain C residue 66 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396 source Swiss-Prot : SWS_FT_FI1 71) chain C residue 103 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396 source Swiss-Prot : SWS_FT_FI1 72) chain C residue 147 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396 source Swiss-Prot : SWS_FT_FI1 73) chain A residue 17 type BINDING sequence F description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396 source Swiss-Prot : SWS_FT_FI1 74) chain C residue 155 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396 source Swiss-Prot : SWS_FT_FI1 75) chain C residue 200 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396 source Swiss-Prot : SWS_FT_FI1 76) chain A residue 66 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396 source Swiss-Prot : SWS_FT_FI1 77) chain A residue 103 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396 source Swiss-Prot : SWS_FT_FI1 78) chain A residue 147 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396 source Swiss-Prot : SWS_FT_FI1 79) chain A residue 155 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396 source Swiss-Prot : SWS_FT_FI1 80) chain A residue 200 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396 source Swiss-Prot : SWS_FT_FI1 81) chain A residue 125 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 82) chain C residue 125 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 83) chain A residue 81 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 84) chain C residue 81 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 85) chain A residue 249 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI4 86) chain A residue 250 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI4 87) chain C residue 249 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI4 88) chain C residue 250 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI4

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