eF-site ID 1gg5-D PDB Code 1gg5 Chain D 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 D:  VGRRALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESD LYAMNFNPIISRKDITGKLKDPANFQYPAESVLAYKEGHL SPDIVAEQKKLEAADLVIFQFPLQWFGVPAILKGWFERVF IGEFAYTYAAMYDKGPFRSKKAVLSITTGGSGSMYSLQGI HGDMNVILWPIQSGILHFCGFQVLEPQLTYSIGHTPADAR IQILEGWKKRLENIWDETPLYFAPSSLFDLNFQAGFLMKK EVQDEEKNKKFGLSVGHHLGKSIPTDNQIKARK Description Functional site 1) chain D residue 66 type sequence Q description BINDING SITE FOR RESIDUE FAD B 602 source : AC2 2) chain D residue 67 type sequence Y description BINDING SITE FOR RESIDUE FAD B 602 source : AC2 3) chain D residue 11 type sequence H description BINDING SITE FOR RESIDUE FAD D 604 source : AC4 4) chain D residue 15 type sequence T description BINDING SITE FOR RESIDUE FAD D 604 source : AC4 5) chain D residue 16 type sequence S description BINDING SITE FOR RESIDUE FAD D 604 source : AC4 6) chain D residue 17 type sequence F description BINDING SITE FOR RESIDUE FAD D 604 source : AC4 7) chain D residue 18 type sequence N description BINDING SITE FOR RESIDUE FAD D 604 source : AC4 8) chain D residue 20 type sequence A description BINDING SITE FOR RESIDUE FAD D 604 source : AC4 9) chain D residue 102 type sequence P description BINDING SITE FOR RESIDUE FAD D 604 source : AC4 10) chain D residue 103 type sequence L description BINDING SITE FOR RESIDUE FAD D 604 source : AC4 11) chain D residue 104 type sequence Q description BINDING SITE FOR RESIDUE FAD D 604 source : AC4 12) chain D residue 105 type sequence W description BINDING SITE FOR RESIDUE FAD D 604 source : AC4 13) chain D residue 106 type sequence F description BINDING SITE FOR RESIDUE FAD D 604 source : AC4 14) chain D residue 147 type sequence T description BINDING SITE FOR RESIDUE FAD D 604 source : AC4 15) chain D residue 148 type sequence T description BINDING SITE FOR RESIDUE FAD D 604 source : AC4 16) chain D residue 149 type sequence G description BINDING SITE FOR RESIDUE FAD D 604 source : AC4 17) chain D residue 150 type sequence G description BINDING SITE FOR RESIDUE FAD D 604 source : AC4 18) chain D residue 155 type sequence Y description BINDING SITE FOR RESIDUE FAD D 604 source : AC4 19) chain D residue 192 type sequence I description BINDING SITE FOR RESIDUE FAD D 604 source : AC4 20) chain D residue 200 type sequence R description BINDING SITE FOR RESIDUE FAD D 604 source : AC4 21) chain D residue 68 type sequence P description BINDING SITE FOR RESIDUE E09 D 702 source : AC6 22) chain D residue 126 type sequence Y description BINDING SITE FOR RESIDUE E09 D 702 source : AC6 23) chain D residue 128 type sequence Y description BINDING SITE FOR RESIDUE E09 D 702 source : AC6 24) chain D residue 178 type sequence F description BINDING SITE FOR RESIDUE E09 D 702 source : AC6 25) chain D residue 106 type sequence F description BINDING SITE FOR RESIDUE E09 B 704 source : AC8 26) chain D residue 149 type sequence G description BINDING SITE FOR RESIDUE E09 B 704 source : AC8 27) chain D residue 150 type sequence G description BINDING SITE FOR RESIDUE E09 B 704 source : AC8 28) chain D residue 161 type sequence H description BINDING SITE FOR RESIDUE E09 B 704 source : AC8 29) chain D residue 149 type catalytic sequence G description 3 source MCSA : MCSA4 30) chain D residue 155 type catalytic sequence Y description 3 source MCSA : MCSA4 31) chain D residue 161 type catalytic sequence H description 3 source MCSA : MCSA4 32) chain D 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 33) chain D 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 34) chain D 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 35) chain D 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 36) chain D 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 37) chain D 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 38) chain D 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 39) chain D residue 125 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 40) chain D residue 81 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 41) chain D 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 42) chain D 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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