eF-site ID 1gg5-C PDB Code 1gg5 Chain 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 C:  VGRRALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESD LYAMNFNPIISRKDITGKLKDPANFQYPAESVLAYKEGHL SPDIVAEQKKLEAADLVIFQFPLQWFGVPAILKGWFERVF IGEFAYTYAAMYDKGPFRSKKAVLSITTGGSGSMYSLQGI HGDMNVILWPIQSGILHFCGFQVLEPQLTYSIGHTPADAR IQILEGWKKRLENIWDETPLYFAPSSLFDLNFQAGFLMKK EVQDEEKNKKFGLSVGHHLGKSIPTDNQIKARK Description Functional site 1) chain C residue 66 type sequence Q description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 2) chain C residue 67 type sequence Y description BINDING SITE FOR RESIDUE FAD A 601 source : AC1 3) chain C residue 11 type sequence H description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 4) chain C residue 15 type sequence T description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 5) chain C residue 16 type sequence S description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 6) chain C residue 17 type sequence F description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 7) chain C residue 18 type sequence N description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 8) chain C residue 20 type sequence A description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 9) chain C residue 102 type sequence P description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 10) chain C residue 103 type sequence L description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 11) chain C residue 104 type sequence Q description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 12) chain C residue 105 type sequence W description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 13) chain C residue 106 type sequence F description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 14) chain C residue 147 type sequence T description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 15) chain C residue 148 type sequence T description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 16) chain C residue 149 type sequence G description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 17) chain C residue 150 type sequence G description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 18) chain C residue 155 type sequence Y description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 19) chain C residue 192 type sequence I description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 20) chain C residue 200 type sequence R description BINDING SITE FOR RESIDUE FAD C 603 source : AC3 21) chain C residue 68 type sequence P description BINDING SITE FOR RESIDUE E09 C 701 source : AC5 22) chain C residue 126 type sequence Y description BINDING SITE FOR RESIDUE E09 C 701 source : AC5 23) chain C residue 128 type sequence Y description BINDING SITE FOR RESIDUE E09 C 701 source : AC5 24) chain C residue 174 type sequence G description BINDING SITE FOR RESIDUE E09 C 701 source : AC5 25) chain C residue 178 type sequence F description BINDING SITE FOR RESIDUE E09 C 701 source : AC5 26) chain C residue 106 type sequence F description BINDING SITE FOR RESIDUE E09 A 703 source : AC7 27) chain C residue 149 type sequence G description BINDING SITE FOR RESIDUE E09 A 703 source : AC7 28) chain C residue 150 type sequence G description BINDING SITE FOR RESIDUE E09 A 703 source : AC7 29) chain C residue 161 type sequence H description BINDING SITE FOR RESIDUE E09 A 703 source : AC7 30) chain C residue 149 type catalytic sequence G description 3 source MCSA : MCSA3 31) chain C residue 155 type catalytic sequence Y description 3 source MCSA : MCSA3 32) chain C residue 161 type catalytic sequence H description 3 source MCSA : MCSA3 33) 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 34) 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 35) 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 36) 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 37) 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 38) 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 39) 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 40) chain C residue 125 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 41) chain C residue 81 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 42) 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 43) 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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