eF-site ID 1r9y-A PDB Code 1r9y Chain A click to enlarge Title Bacterial cytosine deaminase D314A mutant. Classification HYDROLASE Compound Cytosine deaminase Source null (CODA_ECOLI) Sequence A:  ALQTIINARLPGEEGLWQIHLQDGKISAIDAQSGVMPITE NSLDAEQGLVIPPFVEPHIHLDTTQTAGQPNWNQSGTLFE GIERWAERKALLTHDDVKQRAWQTLKWQIANGIQHVRTHV DVSDATLTALKAMLEVKQEVAPWIDLQIVAFPQEGILSYP NGEALLEEALRLGADVVGAIPHFEFTREYGVESLHKTFAL AQKYDRLIDVHCDEIDDEQSRFVETVAALAHHEGMGARVT ASHTTAMHSYNGAYTSRLFRLLKMSGINFVANPLVNIHLQ GRFDTYPKRRGITRVKEMLESGINVCFGHDAVFDPWYPLG TANMLQVLHMGLHVCQLMGYGQINDGLNLITHHSARTLNL QDYGIAAGNSANLIILPAENGFDALRRQVPVRYSVRGGKV IASTQPAQTTVYLEQPEAIDYKR Description Functional site 1) chain A residue 61 type sequence H description BINDING SITE FOR RESIDUE FE A 501 source : AC1 2) chain A residue 63 type sequence H description BINDING SITE FOR RESIDUE FE A 501 source : AC1 3) chain A residue 214 type sequence H description BINDING SITE FOR RESIDUE FE A 501 source : AC1 4) chain A residue 313 type sequence D description BINDING SITE FOR RESIDUE FE A 501 source : AC1 5) chain A residue 128 type sequence A description BINDING SITE FOR RESIDUE GOL A 503 source : AC3 6) chain A residue 134 type sequence K description BINDING SITE FOR RESIDUE GOL A 503 source : AC3 7) chain A residue 171 type sequence E description BINDING SITE FOR RESIDUE GOL A 503 source : AC3 8) chain A residue 174 type sequence R description BINDING SITE FOR RESIDUE GOL A 503 source : AC3 9) chain A residue 175 type sequence L description BINDING SITE FOR RESIDUE GOL A 503 source : AC3 10) chain A residue 245 type SITE sequence S description Activates the nucleophilic water => ECO:0000305|PubMed:21545144, ECO:0000305|PubMed:21604715 source Swiss-Prot : SWS_FT_FI5 11) chain A residue 216 type ACT_SITE sequence D description Proton donor => ECO:0000305|PubMed:11812140, ECO:0000305|PubMed:21545144, ECO:0000305|PubMed:21604715 source Swiss-Prot : SWS_FT_FI1 12) chain A residue 60 type BINDING sequence P description BINDING => ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|Ref.14 source Swiss-Prot : SWS_FT_FI2 13) chain A residue 62 type BINDING sequence I description BINDING => ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|Ref.14 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 213 type BINDING sequence V description BINDING => ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|Ref.14 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 312 type BINDING sequence H description BINDING => ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|Ref.14 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 155 type BINDING sequence P description BINDING => ECO:0000269|PubMed:11812140, ECO:0000269|PubMed:15381761, ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 318 type BINDING sequence P description BINDING => ECO:0000269|PubMed:11812140, ECO:0000269|PubMed:15381761, ECO:0000269|PubMed:21545144 source Swiss-Prot : SWS_FT_FI4 18) chain A residue 216 type catalytic sequence D description 710 source MCSA : MCSA1 19) chain A residue 312 type catalytic sequence H description 710 source MCSA : MCSA1 20) chain A residue 60 type catalytic sequence P description 710 source MCSA : MCSA1 21) chain A residue 62 type catalytic sequence I description 710 source MCSA : MCSA1 22) chain A residue 155 type catalytic sequence P description 710 source MCSA : MCSA1 23) chain A residue 213 type catalytic sequence V description 710 source MCSA : MCSA1

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