eF-site ID 4zvn-B PDB Code 4zvn Chain B click to enlarge Title Reduced quinone reductase 2 in complex with acridine orange Classification Oxidoreductase/oxidoreductase Inhibitor Compound Ribosyldihydronicotinamide dehydrogenase [quinone] Source Homo sapiens (Human) (NQO2_HUMAN) Sequence B:  AGKKVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSD LYAMNFEPRATDKDITGTLSNPEVFNYGVETHEAYKQRSL ASDITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRVL CQGFAFDIPGFYDSGLLQGKLALLSVTTGGTAEMYTKTGV NGDSRYFLWPLQHGTLHFCGFKVLAPQISFAPEIASEEER KGMVAAWSQRLQTIWKEEPIPCTAHWHFGQ Description Functional site 1) chain B residue 66 type sequence N description binding site for residue FAD A 302 source : AC2 2) chain B residue 117 type sequence D description binding site for residue FAD A 302 source : AC2 3) chain B residue 126 type sequence F description binding site for residue AO A 303 source : AC3 4) chain B residue 178 type sequence F description binding site for residue AO A 303 source : AC3 5) chain B residue 173 type sequence H description binding site for residue ZN B 301 source : AC4 6) chain B residue 177 type sequence H description binding site for residue ZN B 301 source : AC4 7) chain B residue 222 type sequence C description binding site for residue ZN B 301 source : AC4 8) chain B residue 11 type sequence H description binding site for residue FAD B 302 source : AC5 9) chain B residue 15 type sequence K description binding site for residue FAD B 302 source : AC5 10) chain B residue 16 type sequence S description binding site for residue FAD B 302 source : AC5 11) chain B residue 17 type sequence F description binding site for residue FAD B 302 source : AC5 12) chain B residue 18 type sequence N description binding site for residue FAD B 302 source : AC5 13) chain B residue 20 type sequence S description binding site for residue FAD B 302 source : AC5 14) chain B residue 102 type sequence P description binding site for residue FAD B 302 source : AC5 15) chain B residue 103 type sequence L description binding site for residue FAD B 302 source : AC5 16) chain B residue 104 type sequence Y description binding site for residue FAD B 302 source : AC5 17) chain B residue 105 type sequence W description binding site for residue FAD B 302 source : AC5 18) chain B residue 106 type sequence F description binding site for residue FAD B 302 source : AC5 19) chain B residue 147 type sequence T description binding site for residue FAD B 302 source : AC5 20) chain B residue 148 type sequence T description binding site for residue FAD B 302 source : AC5 21) chain B residue 149 type sequence G description binding site for residue FAD B 302 source : AC5 22) chain B residue 150 type sequence G description binding site for residue FAD B 302 source : AC5 23) chain B residue 155 type sequence Y description binding site for residue FAD B 302 source : AC5 24) chain B residue 193 type sequence E description binding site for residue FAD B 302 source : AC5 25) chain B residue 200 type sequence R description binding site for residue FAD B 302 source : AC5 26) chain B residue 201 type sequence K description binding site for residue FAD B 302 source : AC5 27) chain B residue 105 type sequence W description binding site for residue AO B 303 source : AC6 28) chain B residue 149 type sequence G description binding site for residue AO B 303 source : AC6 29) chain B residue 150 type sequence G description binding site for residue AO B 303 source : AC6 30) chain B residue 72 type sequence H description binding site for residue ZN B 304 source : AC7 31) chain B residue 127 type sequence D description binding site for residue ZN B 304 source : AC7 32) chain B residue 218 type sequence E description binding site for residue ZN B 304 source : AC7 33) chain B residue 103 type BINDING sequence L description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 34) chain B residue 147 type BINDING sequence T description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 35) chain B residue 155 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 36) chain B residue 193 type BINDING sequence E description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 37) chain B residue 200 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 38) chain B residue 11 type BINDING sequence H description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 39) chain B residue 17 type BINDING sequence F description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 40) chain B residue 196 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI3 41) chain B residue 79 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI3 42) chain B residue 177 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 43) chain B residue 222 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 44) chain B residue 126 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 45) chain B residue 173 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2

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