eF-site ID 4u7h-A PDB Code 4u7h Chain A click to enlarge Title Oxidized 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 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 15 type sequence K description binding site for residue FAD A 302 source : AC2 6) chain A residue 16 type sequence S description binding site for residue FAD A 302 source : AC2 7) chain A residue 17 type sequence F description binding site for residue FAD A 302 source : AC2 8) chain A residue 18 type sequence N description binding site for residue FAD A 302 source : AC2 9) chain A residue 20 type sequence S description binding site for residue FAD A 302 source : AC2 10) chain A residue 102 type sequence P description binding site for residue FAD A 302 source : AC2 11) chain A residue 103 type sequence L description binding site for residue FAD A 302 source : AC2 12) chain A residue 104 type sequence Y description binding site for residue FAD A 302 source : AC2 13) chain A residue 105 type sequence W description binding site for residue FAD A 302 source : AC2 14) chain A residue 106 type sequence F description binding site for residue FAD A 302 source : AC2 15) chain A residue 147 type sequence T description binding site for residue FAD A 302 source : AC2 16) chain A residue 148 type sequence T description binding site for residue FAD A 302 source : AC2 17) chain A residue 149 type sequence G description binding site for residue FAD A 302 source : AC2 18) chain A residue 150 type sequence G description binding site for residue FAD A 302 source : AC2 19) chain A residue 155 type sequence Y description binding site for residue FAD A 302 source : AC2 20) chain A residue 193 type sequence E description binding site for residue FAD A 302 source : AC2 21) chain A residue 200 type sequence R description binding site for residue FAD A 302 source : AC2 22) chain A residue 105 type sequence W description binding site for residue K25 B 301 source : AC3 23) chain A residue 150 type sequence G description binding site for residue K25 B 301 source : AC3 24) chain A residue 161 type sequence N description binding site for residue K25 B 301 source : AC3 25) chain A residue 66 type sequence N description binding site for residue FAD B 303 source : AC5 26) chain A residue 117 type sequence D description binding site for residue FAD B 303 source : AC5 27) chain A residue 126 type sequence F description binding site for residue K25 B 304 source : AC6 28) chain A residue 174 type sequence G description binding site for residue K25 B 304 source : AC6 29) chain A residue 178 type sequence F description binding site for residue K25 B 304 source : AC6 30) chain A residue 11 type BINDING sequence H description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 17 type BINDING sequence F description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 103 type BINDING sequence L description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 147 type BINDING sequence T description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 155 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 35) chain A residue 193 type BINDING sequence E description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 200 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 126 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 38) chain A residue 173 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 39) chain A residue 177 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 40) chain A residue 222 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 41) chain A residue 79 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI3 42) chain A residue 196 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI3

Display surface Download Links