eF-site ID 4u7f-AB PDB Code 4u7f Chain A, B click to enlarge Title Reduced quinone reductase 2 in complex with CK2 inhibitor DMAT Classification Oxidoreductase/Inhibitor Compound Ribosyldihydronicotinamide dehydrogenase [quinone] 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 301 source : AC1 2) chain A residue 177 type sequence H description binding site for residue ZN A 301 source : AC1 3) chain A residue 222 type sequence C description binding site for residue ZN A 301 source : AC1 4) chain A residue 11 type sequence H description binding site for residue FAD A 302 source : AC2 5) chain A residue 16 type sequence S description binding site for residue FAD A 302 source : AC2 6) chain A residue 17 type sequence F description binding site for residue FAD A 302 source : AC2 7) chain A residue 18 type sequence N description binding site for residue FAD A 302 source : AC2 8) chain A residue 20 type sequence S description binding site for residue FAD A 302 source : AC2 9) chain A residue 102 type sequence P description binding site for residue FAD A 302 source : AC2 10) chain A residue 103 type sequence L description binding site for residue FAD A 302 source : AC2 11) chain A residue 104 type sequence Y description binding site for residue FAD A 302 source : AC2 12) chain A residue 105 type sequence W description binding site for residue FAD A 302 source : AC2 13) chain A residue 106 type sequence F description binding site for residue FAD A 302 source : AC2 14) chain A residue 147 type sequence T description binding site for residue FAD A 302 source : AC2 15) chain A residue 148 type sequence T description binding site for residue FAD A 302 source : AC2 16) chain A residue 149 type sequence G description binding site for residue FAD A 302 source : AC2 17) chain A residue 150 type sequence G description binding site for residue FAD A 302 source : AC2 18) chain A residue 155 type sequence Y description binding site for residue FAD A 302 source : AC2 19) chain A residue 193 type sequence E description binding site for residue FAD A 302 source : AC2 20) chain A residue 200 type sequence R description binding site for residue FAD A 302 source : AC2 21) chain A residue 201 type sequence K description binding site for residue FAD A 302 source : AC2 22) chain B residue 66 type sequence N description binding site for residue FAD A 302 source : AC2 23) chain B residue 117 type sequence D description binding site for residue FAD A 302 source : AC2 24) chain A residue 105 type sequence W description binding site for residue K25 B 301 source : AC3 25) chain A residue 149 type sequence G description binding site for residue K25 B 301 source : AC3 26) chain A residue 150 type sequence G description binding site for residue K25 B 301 source : AC3 27) chain A residue 193 type sequence E description binding site for residue K25 B 301 source : AC3 28) chain B residue 66 type sequence N description binding site for residue K25 B 301 source : AC3 29) chain B residue 68 type sequence G description binding site for residue K25 B 301 source : AC3 30) chain B residue 69 type sequence V description binding site for residue K25 B 301 source : AC3 31) chain B residue 126 type sequence F description binding site for residue K25 B 301 source : AC3 32) chain B residue 178 type sequence F description binding site for residue K25 B 301 source : AC3 33) chain B residue 173 type sequence H description binding site for residue ZN B 302 source : AC4 34) chain B residue 177 type sequence H description binding site for residue ZN B 302 source : AC4 35) chain B residue 222 type sequence C description binding site for residue ZN B 302 source : AC4 36) chain A residue 66 type sequence N description binding site for residue FAD B 303 source : AC5 37) chain A residue 117 type sequence D description binding site for residue FAD B 303 source : AC5 38) chain B residue 11 type sequence H description binding site for residue FAD B 303 source : AC5 39) chain B residue 15 type sequence K description binding site for residue FAD B 303 source : AC5 40) chain B residue 16 type sequence S description binding site for residue FAD B 303 source : AC5 41) chain B residue 17 type sequence F description binding site for residue FAD B 303 source : AC5 42) chain B residue 18 type sequence N description binding site for residue FAD B 303 source : AC5 43) chain B residue 20 type sequence S description binding site for residue FAD B 303 source : AC5 44) chain B residue 102 type sequence P description binding site for residue FAD B 303 source : AC5 45) chain B residue 103 type sequence L description binding site for residue FAD B 303 source : AC5 46) chain B residue 104 type sequence Y description binding site for residue FAD B 303 source : AC5 47) chain B residue 105 type sequence W description binding site for residue FAD B 303 source : AC5 48) chain B residue 106 type sequence F description binding site for residue FAD B 303 source : AC5 49) chain B residue 147 type sequence T description binding site for residue FAD B 303 source : AC5 50) chain B residue 148 type sequence T description binding site for residue FAD B 303 source : AC5 51) chain B residue 149 type sequence G description binding site for residue FAD B 303 source : AC5 52) chain B residue 150 type sequence G description binding site for residue FAD B 303 source : AC5 53) chain B residue 155 type sequence Y description binding site for residue FAD B 303 source : AC5 54) chain B residue 193 type sequence E description binding site for residue FAD B 303 source : AC5 55) chain B residue 200 type sequence R description binding site for residue FAD B 303 source : AC5 56) chain A residue 68 type sequence G description binding site for residue K25 B 304 source : AC6 57) chain A residue 126 type sequence F description binding site for residue K25 B 304 source : AC6 58) chain A residue 178 type sequence F description binding site for residue K25 B 304 source : AC6 59) chain B residue 105 type sequence W description binding site for residue K25 B 304 source : AC6 60) chain B residue 149 type sequence G description binding site for residue K25 B 304 source : AC6 61) chain B residue 193 type sequence E description binding site for residue K25 B 304 source : AC6 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 200 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 68) chain B residue 11 type BINDING sequence H description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 69) chain B residue 17 type BINDING sequence F description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 70) chain A residue 11 type BINDING sequence H description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 71) chain A residue 17 type BINDING sequence F description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 72) chain A residue 103 type BINDING sequence L description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 73) chain A residue 147 type BINDING sequence T description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 74) chain A residue 155 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 75) chain A residue 193 type BINDING sequence E description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 76) chain B residue 196 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI3 77) chain A residue 79 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI3 78) chain A residue 196 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI3 79) chain B residue 79 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI3 80) chain B residue 177 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 81) chain B residue 222 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 82) chain B residue 126 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 83) chain B residue 173 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 84) chain A residue 126 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 85) chain A residue 173 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 86) chain A residue 177 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 87) chain A residue 222 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2

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