eF-site ID 2qmz-AB PDB Code 2qmz Chain A, B click to enlarge Title Quinone Reductase 2 in Complex with Dopamine Classification OXIDOREDUCTASE Compound Ribosyldihydronicotinamide dehydrogenase Source Homo sapiens (Human) (NQO2_HUMAN) Sequence A:  AGKKVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSD LYAMNFEPRATDKDITGTLSNPEVFNYGVETHEAYKQRSL ASDITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRVL CQGFAFDIPGFYDSGLLQGKLALLSVTTGGTAEMYTKTGV NGDSRYFLWPLQHGTLHFCGFKVLAPQISFAPEIASEEER KGMVAAWSQRLQTIWKEEPIPCTAHWHFGQ B:  AGKKVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSD LYAMNFEPRATDKDITGTLSNPEVFNYGVETHEAYKQRSL ASDITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRVL CQGFAFDIPGFYDSGLLQGKLALLSVTTGGTAEMYTKTGV NGDSRYFLWPLQHGTLHFCGFKVLAPQISFAPEIASEEER KGMVAAWSQRLQTIWKEEPIPCTAHWHFGQ Description Functional site 1) chain A residue 173 type sequence H description BINDING SITE FOR RESIDUE ZN A 231 source : AC1 2) chain A residue 177 type sequence H description BINDING SITE FOR RESIDUE ZN A 231 source : AC1 3) chain A residue 222 type sequence C description BINDING SITE FOR RESIDUE ZN A 231 source : AC1 4) chain B residue 173 type sequence H description BINDING SITE FOR RESIDUE ZN B 232 source : AC2 5) chain B residue 177 type sequence H description BINDING SITE FOR RESIDUE ZN B 232 source : AC2 6) chain B residue 222 type sequence C description BINDING SITE FOR RESIDUE ZN B 232 source : AC2 7) chain A residue 66 type sequence N description BINDING SITE FOR RESIDUE FAD B 233 source : AC3 8) chain A residue 117 type sequence D description BINDING SITE FOR RESIDUE FAD B 233 source : AC3 9) chain B residue 11 type sequence H description BINDING SITE FOR RESIDUE FAD B 233 source : AC3 10) chain B residue 15 type sequence K description BINDING SITE FOR RESIDUE FAD B 233 source : AC3 11) chain B residue 16 type sequence S description BINDING SITE FOR RESIDUE FAD B 233 source : AC3 12) chain B residue 17 type sequence F description BINDING SITE FOR RESIDUE FAD B 233 source : AC3 13) chain B residue 18 type sequence N description BINDING SITE FOR RESIDUE FAD B 233 source : AC3 14) chain B residue 20 type sequence S description BINDING SITE FOR RESIDUE FAD B 233 source : AC3 15) chain B residue 102 type sequence P description BINDING SITE FOR RESIDUE FAD B 233 source : AC3 16) chain B residue 103 type sequence L description BINDING SITE FOR RESIDUE FAD B 233 source : AC3 17) chain B residue 104 type sequence Y description BINDING SITE FOR RESIDUE FAD B 233 source : AC3 18) chain B residue 105 type sequence W description BINDING SITE FOR RESIDUE FAD B 233 source : AC3 19) chain B residue 106 type sequence F description BINDING SITE FOR RESIDUE FAD B 233 source : AC3 20) chain B residue 147 type sequence T description BINDING SITE FOR RESIDUE FAD B 233 source : AC3 21) chain B residue 148 type sequence T description BINDING SITE FOR RESIDUE FAD B 233 source : AC3 22) chain B residue 149 type sequence G description BINDING SITE FOR RESIDUE FAD B 233 source : AC3 23) chain B residue 150 type sequence G description BINDING SITE FOR RESIDUE FAD B 233 source : AC3 24) chain B residue 155 type sequence Y description BINDING SITE FOR RESIDUE FAD B 233 source : AC3 25) chain B residue 193 type sequence E description BINDING SITE FOR RESIDUE FAD B 233 source : AC3 26) chain B residue 197 type sequence E description BINDING SITE FOR RESIDUE FAD B 233 source : AC3 27) chain B residue 200 type sequence R description BINDING SITE FOR RESIDUE FAD B 233 source : AC3 28) chain A residue 11 type sequence H description BINDING SITE FOR RESIDUE FAD A 234 source : AC4 29) chain A residue 15 type sequence K description BINDING SITE FOR RESIDUE FAD A 234 source : AC4 30) chain A residue 16 type sequence S description BINDING SITE FOR RESIDUE FAD A 234 source : AC4 31) chain A residue 17 type sequence F description BINDING SITE FOR RESIDUE FAD A 234 source : AC4 32) chain A residue 18 type sequence N description BINDING SITE FOR RESIDUE FAD A 234 source : AC4 33) chain A residue 20 type sequence S description BINDING SITE FOR RESIDUE FAD A 234 source : AC4 34) chain A residue 102 type sequence P description BINDING SITE FOR RESIDUE FAD A 234 source : AC4 35) chain A residue 103 type sequence L description BINDING SITE FOR RESIDUE FAD A 234 source : AC4 36) chain A residue 104 type sequence Y description BINDING SITE FOR RESIDUE FAD A 234 source : AC4 37) chain A residue 105 type sequence W description BINDING SITE FOR RESIDUE FAD A 234 source : AC4 38) chain A residue 106 type sequence F description BINDING SITE FOR RESIDUE FAD A 234 source : AC4 39) chain A residue 147 type sequence T description BINDING SITE FOR RESIDUE FAD A 234 source : AC4 40) chain A residue 148 type sequence T description BINDING SITE FOR RESIDUE FAD A 234 source : AC4 41) chain A residue 149 type sequence G description BINDING SITE FOR RESIDUE FAD A 234 source : AC4 42) chain A residue 150 type sequence G description BINDING SITE FOR RESIDUE FAD A 234 source : AC4 43) chain A residue 155 type sequence Y description BINDING SITE FOR RESIDUE FAD A 234 source : AC4 44) chain A residue 193 type sequence E description BINDING SITE FOR RESIDUE FAD A 234 source : AC4 45) chain A residue 200 type sequence R description BINDING SITE FOR RESIDUE FAD A 234 source : AC4 46) chain A residue 201 type sequence K description BINDING SITE FOR RESIDUE FAD A 234 source : AC4 47) chain B residue 66 type sequence N description BINDING SITE FOR RESIDUE FAD A 234 source : AC4 48) chain B residue 117 type sequence D description BINDING SITE FOR RESIDUE FAD A 234 source : AC4 49) chain A residue 105 type sequence W description BINDING SITE FOR RESIDUE LDP A 501 source : AC5 50) chain B residue 68 type sequence G description BINDING SITE FOR RESIDUE LDP A 501 source : AC5 51) chain B residue 122 type sequence Q description BINDING SITE FOR RESIDUE LDP A 501 source : AC5 52) chain B residue 126 type sequence F description BINDING SITE FOR RESIDUE LDP A 501 source : AC5 53) chain B residue 128 type sequence I description BINDING SITE FOR RESIDUE LDP A 501 source : AC5 54) chain B residue 178 type sequence F description BINDING SITE FOR RESIDUE LDP A 501 source : AC5 55) chain A residue 122 type sequence Q description BINDING SITE FOR RESIDUE LDP B 502 source : AC6 56) chain A residue 126 type sequence F description BINDING SITE FOR RESIDUE LDP B 502 source : AC6 57) chain A residue 178 type sequence F description BINDING SITE FOR RESIDUE LDP B 502 source : AC6 58) chain B residue 105 type sequence W description BINDING SITE FOR RESIDUE LDP B 502 source : AC6 59) chain B residue 149 type sequence G description BINDING SITE FOR RESIDUE LDP B 502 source : AC6 60) chain B residue 150 type sequence G description BINDING SITE FOR RESIDUE LDP B 502 source : AC6 61) chain A residue 11 type BINDING sequence H description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 62) chain B residue 103 type BINDING sequence L description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 63) chain B residue 147 type BINDING sequence T description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 64) chain B residue 155 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 65) chain B residue 193 type BINDING sequence E description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 66) chain B residue 200 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 67) chain A residue 17 type BINDING sequence F description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 68) chain A residue 103 type BINDING sequence L description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 69) chain A residue 147 type BINDING sequence T description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 70) chain A residue 155 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 71) chain A residue 193 type BINDING sequence E description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 72) chain A residue 200 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 73) chain B residue 11 type BINDING sequence H description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 74) chain B residue 17 type BINDING sequence F description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 75) chain A residue 126 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 76) chain A residue 173 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 77) chain A residue 177 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 78) chain A residue 222 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 79) chain B residue 126 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 80) chain B residue 173 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 81) chain B residue 177 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 82) chain B residue 222 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 83) chain A residue 79 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI3 84) chain A residue 196 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI3 85) chain B residue 79 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI3 86) chain B residue 196 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI3

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