eF-site ID 2h0r-ABCDEFG PDB Code 2h0r Chain A, B, C, D, E, F, G click to enlarge Title Structure of the Yeast Nicotinamidase Pnc1p Classification HYDROLASE Compound Nicotinamidase Source ORGANISM_COMMON: baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae; Sequence A:  MKTLIVVDMQNDFISPLGSLTVPKGEELINPISDLMQDAD RDWHRIVVTRDWHPSRHISFAKNHKDKEPYSTYTYHSPRP GDDSTQEGILWPVHCVKNTWGSQLVDQIMDQVVTKHIKIV DKGFLTDREYYSAFHDIWNFHKTDMNKYLEKHHTDEVYIV GVALEYCVKATAISAAELGYKTTVLLDYTRPISDDPEVIN KVKEELKAHNINVVDK B:  MKTLIVVDMQNDFISPLGSLTVPKGEELINPISDLMQDAD RDWHRIVVTRDWHPSRHISFAKNHKDKEPYSTYTYHSPRP GDDSTQEGILWPVHCVKNTWGSQLVDQIMDQVVTKHIKIV DKGFLTDREYYSAFHDIWNFHKTDMNKYLEKHHTDEVYIV GVALEYCVKATAISAAELGYKTTVLLDYTRPISDDPEVIN KVKEELKAHNINVVDK C:  MKTLIVVDMQNDFISPLGSLTVPKGEELINPISDLMQDAD RDWHRIVVTRDWHPSRHISFAKNHKDKEPYSTYTYHSPRP GDDSTQEGILWPVHCVKNTWGSQLVDQIMDQVVTKHIKIV DKGFLTDREYYSAFHDIWNFHKTDMNKYLEKHHTDEVYIV GVALEYCVKATAISAAELGYKTTVLLDYTRPISDDPEVIN KVKEELKAHNINVVDK D:  MKTLIVVDMQNDFISPLGSLTVPKGEELINPISDLMQDAD RDWHRIVVTRDWHPSRHISFAKNHKDKEPYSTYTYHSPRP GDDSTQEGILWPVHCVKNTWGSQLVDQIMDQVVTKHIKIV DKGFLTDREYYSAFHDIWNFHKTDMNKYLEKHHTDEVYIV GVALEYCVKATAISAAELGYKTTVLLDYTRPISDDPEVIN KVKEELKAHNINVVDK E:  MKTLIVVDMQNDFISPLGSLTVPKGEELINPISDLMQDAD RDWHRIVVTRDWHPSRHISFAKNHKDKEPYSTYTYHSPRP GDDSTQEGILWPVHCVKNTWGSQLVDQIMDQVVTKHIKIV DKGFLTDREYYSAFHDIWNFHKTDMNKYLEKHHTDEVYIV GVALEYCVKATAISAAELGYKTTVLLDYTRPISDDPEVIN KVKEELKAHNINVVDK F:  MKTLIVVDMQNDFISPLGSLTVPKGEELINPISDLMQDAD RDWHRIVVTRDWHPSRHISFAKNHKDKEPYSTYTYHSPRP GDDSTQEGILWPVHCVKNTWGSQLVDQIMDQVVTKHIKIV DKGFLTDREYYSAFHDIWNFHKTDMNKYLEKHHTDEVYIV GVALEYCVKATAISAAELGYKTTVLLDYTRPISDDPEVIN KVKEELKAHNINVVDK G:  MKTLIVVDMQNDFISPLGSLTVPKGEELINPISDLMQDAD RDWHRIVVTRDWHPSRHISFAKNHKDKEPYSTYTYHSPRP GDDSTQEGILWPVHCVKNTWGSQLVDQIMDQVVTKHIKIV DKGFLTDREYYSAFHDIWNFHKTDMNKYLEKHHTDEVYIV GVALEYCVKATAISAAELGYKTTVLLDYTRPISDDPEVIN KVKEELKAHNINVVDK Description Functional site 1) chain A residue 51 type sequence D description BINDING SITE FOR RESIDUE ZN A 301 source : AC1 2) chain A residue 53 type sequence H description BINDING SITE FOR RESIDUE ZN A 301 source : AC1 3) chain A residue 94 type sequence H description BINDING SITE FOR RESIDUE ZN A 301 source : AC1 4) chain B residue 51 type sequence D description BINDING SITE FOR RESIDUE ZN B 301 source : AC2 5) chain B residue 53 type sequence H description BINDING SITE FOR RESIDUE ZN B 301 source : AC2 6) chain B residue 94 type sequence H description BINDING SITE FOR RESIDUE ZN B 301 source : AC2 7) chain C residue 51 type sequence D description BINDING SITE FOR RESIDUE ZN C 301 source : AC3 8) chain C residue 53 type sequence H description BINDING SITE FOR RESIDUE ZN C 301 source : AC3 9) chain C residue 94 type sequence H description BINDING SITE FOR RESIDUE ZN C 301 source : AC3 10) chain D residue 51 type sequence D description BINDING SITE FOR RESIDUE ZN D 301 source : AC4 11) chain D residue 53 type sequence H description BINDING SITE FOR RESIDUE ZN D 301 source : AC4 12) chain D residue 94 type sequence H description BINDING SITE FOR RESIDUE ZN D 301 source : AC4 13) chain E residue 51 type sequence D description BINDING SITE FOR RESIDUE ZN E 301 source : AC5 14) chain E residue 53 type sequence H description BINDING SITE FOR RESIDUE ZN E 301 source : AC5 15) chain E residue 94 type sequence H description BINDING SITE FOR RESIDUE ZN E 301 source : AC5 16) chain E residue 129 type sequence E description BINDING SITE FOR RESIDUE ZN E 301 source : AC5 17) chain F residue 51 type sequence D description BINDING SITE FOR RESIDUE ZN F 301 source : AC6 18) chain F residue 53 type sequence H description BINDING SITE FOR RESIDUE ZN F 301 source : AC6 19) chain F residue 94 type sequence H description BINDING SITE FOR RESIDUE ZN F 301 source : AC6 20) chain G residue 51 type sequence D description BINDING SITE FOR RESIDUE ZN G 301 source : AC7 21) chain G residue 53 type sequence H description BINDING SITE FOR RESIDUE ZN G 301 source : AC7 22) chain G residue 94 type sequence H description BINDING SITE FOR RESIDUE ZN G 301 source : AC7 23) chain A residue 51 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17382284, ECO:0007744|PDB:2H0R source Swiss-Prot : SWS_FT_FI3 24) chain D residue 51 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17382284, ECO:0007744|PDB:2H0R source Swiss-Prot : SWS_FT_FI3 25) chain D residue 53 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17382284, ECO:0007744|PDB:2H0R source Swiss-Prot : SWS_FT_FI3 26) chain D residue 94 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17382284, ECO:0007744|PDB:2H0R source Swiss-Prot : SWS_FT_FI3 27) chain E residue 51 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17382284, ECO:0007744|PDB:2H0R source Swiss-Prot : SWS_FT_FI3 28) chain E residue 53 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17382284, ECO:0007744|PDB:2H0R source Swiss-Prot : SWS_FT_FI3 29) chain E residue 94 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17382284, ECO:0007744|PDB:2H0R source Swiss-Prot : SWS_FT_FI3 30) chain F residue 51 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17382284, ECO:0007744|PDB:2H0R source Swiss-Prot : SWS_FT_FI3 31) chain F residue 53 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17382284, ECO:0007744|PDB:2H0R source Swiss-Prot : SWS_FT_FI3 32) chain F residue 94 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17382284, ECO:0007744|PDB:2H0R source Swiss-Prot : SWS_FT_FI3 33) chain G residue 51 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17382284, ECO:0007744|PDB:2H0R source Swiss-Prot : SWS_FT_FI3 34) chain A residue 53 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17382284, ECO:0007744|PDB:2H0R source Swiss-Prot : SWS_FT_FI3 35) chain G residue 53 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17382284, ECO:0007744|PDB:2H0R source Swiss-Prot : SWS_FT_FI3 36) chain G residue 94 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17382284, ECO:0007744|PDB:2H0R source Swiss-Prot : SWS_FT_FI3 37) chain A residue 94 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17382284, ECO:0007744|PDB:2H0R source Swiss-Prot : SWS_FT_FI3 38) chain B residue 51 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17382284, ECO:0007744|PDB:2H0R source Swiss-Prot : SWS_FT_FI3 39) chain B residue 53 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17382284, ECO:0007744|PDB:2H0R source Swiss-Prot : SWS_FT_FI3 40) chain B residue 94 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17382284, ECO:0007744|PDB:2H0R source Swiss-Prot : SWS_FT_FI3 41) chain C residue 51 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17382284, ECO:0007744|PDB:2H0R source Swiss-Prot : SWS_FT_FI3 42) chain C residue 53 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17382284, ECO:0007744|PDB:2H0R source Swiss-Prot : SWS_FT_FI3 43) chain C residue 94 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17382284, ECO:0007744|PDB:2H0R source Swiss-Prot : SWS_FT_FI3 44) chain A residue 8 type ACT_SITE sequence D description ACT_SITE => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 45) chain E residue 122 type ACT_SITE sequence K description ACT_SITE => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 46) chain F residue 8 type ACT_SITE sequence D description ACT_SITE => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 47) chain F residue 122 type ACT_SITE sequence K description ACT_SITE => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 48) chain G residue 8 type ACT_SITE sequence D description ACT_SITE => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 49) chain G residue 122 type ACT_SITE sequence K description ACT_SITE => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 50) chain A residue 122 type ACT_SITE sequence K description ACT_SITE => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 51) chain B residue 8 type ACT_SITE sequence D description ACT_SITE => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 52) chain B residue 122 type ACT_SITE sequence K description ACT_SITE => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 53) chain C residue 8 type ACT_SITE sequence D description ACT_SITE => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 54) chain C residue 122 type ACT_SITE sequence K description ACT_SITE => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 55) chain D residue 8 type ACT_SITE sequence D description ACT_SITE => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 56) chain D residue 122 type ACT_SITE sequence K description ACT_SITE => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 57) chain E residue 8 type ACT_SITE sequence D description ACT_SITE => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 58) chain A residue 167 type ACT_SITE sequence C description Nucleophile => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 59) chain B residue 167 type ACT_SITE sequence C description Nucleophile => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 60) chain C residue 167 type ACT_SITE sequence C description Nucleophile => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 61) chain D residue 167 type ACT_SITE sequence C description Nucleophile => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 62) chain E residue 167 type ACT_SITE sequence C description Nucleophile => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 63) chain F residue 167 type ACT_SITE sequence C description Nucleophile => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 64) chain G residue 167 type ACT_SITE sequence C description Nucleophile => ECO:0000255 source Swiss-Prot : SWS_FT_FI2

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