eF-site ID 3o2n-A PDB Code 3o2n Chain A click to enlarge Title X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 Classification OXIDOREDUCTASE Compound Ribosyldihydronicotinamide dehydrogenase [quinone] Source Homo sapiens (Human) (NQO2_HUMAN) Sequence A:  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 A residue 11 type sequence H description BINDING SITE FOR RESIDUE FAD A 232 source : AC2 5) chain A residue 15 type sequence K description BINDING SITE FOR RESIDUE FAD A 232 source : AC2 6) chain A residue 16 type sequence S description BINDING SITE FOR RESIDUE FAD A 232 source : AC2 7) chain A residue 17 type sequence F description BINDING SITE FOR RESIDUE FAD A 232 source : AC2 8) chain A residue 18 type sequence N description BINDING SITE FOR RESIDUE FAD A 232 source : AC2 9) chain A residue 20 type sequence S description BINDING SITE FOR RESIDUE FAD A 232 source : AC2 10) chain A residue 102 type sequence P description BINDING SITE FOR RESIDUE FAD A 232 source : AC2 11) chain A residue 103 type sequence L description BINDING SITE FOR RESIDUE FAD A 232 source : AC2 12) chain A residue 104 type sequence Y description BINDING SITE FOR RESIDUE FAD A 232 source : AC2 13) chain A residue 105 type sequence W description BINDING SITE FOR RESIDUE FAD A 232 source : AC2 14) chain A residue 106 type sequence F description BINDING SITE FOR RESIDUE FAD A 232 source : AC2 15) chain A residue 147 type sequence T description BINDING SITE FOR RESIDUE FAD A 232 source : AC2 16) chain A residue 148 type sequence T description BINDING SITE FOR RESIDUE FAD A 232 source : AC2 17) chain A residue 149 type sequence G description BINDING SITE FOR RESIDUE FAD A 232 source : AC2 18) chain A residue 150 type sequence G description BINDING SITE FOR RESIDUE FAD A 232 source : AC2 19) chain A residue 155 type sequence Y description BINDING SITE FOR RESIDUE FAD A 232 source : AC2 20) chain A residue 193 type sequence E description BINDING SITE FOR RESIDUE FAD A 232 source : AC2 21) chain A residue 200 type sequence R description BINDING SITE FOR RESIDUE FAD A 232 source : AC2 22) chain A residue 201 type sequence K description BINDING SITE FOR RESIDUE FAD A 232 source : AC2 23) chain A residue 122 type sequence Q description BINDING SITE FOR RESIDUE MZX A 233 source : AC3 24) chain A residue 128 type sequence I description BINDING SITE FOR RESIDUE MZX A 233 source : AC3 25) chain A residue 131 type sequence F description BINDING SITE FOR RESIDUE MZX A 233 source : AC3 26) chain A residue 178 type sequence F description BINDING SITE FOR RESIDUE MZX A 233 source : AC3 27) chain A residue 66 type sequence N description BINDING SITE FOR RESIDUE FAD B 232 source : AC5 28) chain A residue 67 type sequence Y description BINDING SITE FOR RESIDUE FAD B 232 source : AC5 29) chain A residue 117 type sequence D description BINDING SITE FOR RESIDUE FAD B 232 source : AC5 30) chain A residue 178 type sequence F description BINDING SITE FOR RESIDUE MZX B 233 source : AC6 31) chain A residue 105 type sequence W description BINDING SITE FOR RESIDUE MZX B 234 source : AC7 32) chain A residue 149 type sequence G description BINDING SITE FOR RESIDUE MZX B 234 source : AC7 33) chain A residue 150 type sequence G description BINDING SITE FOR RESIDUE MZX B 234 source : AC7 34) chain A residue 161 type sequence N description BINDING SITE FOR RESIDUE MZX B 234 source : AC7 35) chain A residue 11 type BINDING sequence H description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 17 type BINDING sequence F description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 103 type BINDING sequence L description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 38) chain A residue 147 type BINDING sequence T description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 155 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 40) chain A residue 193 type BINDING sequence E description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 41) chain A residue 200 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 42) chain A residue 126 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 43) chain A residue 173 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 44) chain A residue 177 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 45) chain A residue 222 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 46) chain A residue 79 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI3 47) chain A residue 196 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI3

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