eF-site ID 1k70-A PDB Code 1k70 Chain A Title The Structure of Escherichia coli Cytosine Deaminase bound to 4-Hydroxy-3,4-Dihydro-1H-Pyrimidin-2-one Classification HYDROLASE Compound Cytosine Deaminase Source Escherichia coli (strain K12) (CODA_ECOLI) Sequence A:  ALQTIINARLPGEEGLWQIHLQDGKISAIDAQSGVMPITE NSLDAEQGLVIPPFVEPHIHLDTTQTAGQPNWNQSGTLFE GIERWAERKALLTHDDVKQRAWQTLKWQIANGIQHVRTHV DVSDATLTALKAMLEVKQEVAPWIDLQIVAFPQEGILSYP NGEALLEEALRLGADVVGAIPHFEFTREYGVESLHKTFAL AQKYDRLIDVHCDEIDDEQSRFVETVAALAHHEGMGARVT ASHTTAMHSYNGAYTSRLFRLLKMSGINFVANPLVNIHLQ GRFDTYPKRRGITRVKEMLESGINVCFGHDDVFDPWYPLG TANMLQVLHMGLHVCQLMGYGQINDGLNLITHHSARTLNL QDYGIAAGNSANLIILPAENGFDALRRQVPVRYSVRGGKV IASTQPAQTTVYLEQPEAIDYKR Description Functional site 1) chain A residue 61 type sequence H description BINDING SITE FOR RESIDUE FE A 502 source : AC1 2) chain A residue 63 type sequence H description BINDING SITE FOR RESIDUE FE A 502 source : AC1 3) chain A residue 214 type sequence H description BINDING SITE FOR RESIDUE FE A 502 source : AC1 4) chain A residue 313 type sequence D description BINDING SITE FOR RESIDUE FE A 502 source : AC1 5) chain A residue 63 type sequence H description BINDING SITE FOR RESIDUE HPY A 501 source : AC2 6) chain A residue 81 type sequence L description BINDING SITE FOR RESIDUE HPY A 501 source : AC2 7) chain A residue 154 type sequence F description BINDING SITE FOR RESIDUE HPY A 501 source : AC2 8) chain A residue 156 type sequence Q description BINDING SITE FOR RESIDUE HPY A 501 source : AC2 9) chain A residue 214 type sequence H description BINDING SITE FOR RESIDUE HPY A 501 source : AC2 10) chain A residue 217 type sequence E description BINDING SITE FOR RESIDUE HPY A 501 source : AC2 11) chain A residue 246 type sequence H description BINDING SITE FOR RESIDUE HPY A 501 source : AC2 12) chain A residue 313 type sequence D description BINDING SITE FOR RESIDUE HPY A 501 source : AC2 13) chain A residue 314 type sequence D description BINDING SITE FOR RESIDUE HPY A 501 source : AC2 14) chain A residue 319 type sequence W description BINDING SITE FOR RESIDUE HPY A 501 source : AC2 15) chain A residue 62 type catalytic sequence I description 710 source MCSA : MCSA1 16) chain A residue 64 type catalytic sequence L description 710 source MCSA : MCSA1 17) chain A residue 157 type catalytic sequence E description 710 source MCSA : MCSA1 18) chain A residue 215 type catalytic sequence C description 710 source MCSA : MCSA1 19) chain A residue 218 type catalytic sequence I description 710 source MCSA : MCSA1 20) chain A residue 314 type catalytic sequence D description 710 source MCSA : MCSA1 21) chain A residue 218 type ACT_SITE sequence I description Proton donor => ECO:0000305|PubMed:11812140, ECO:0000305|PubMed:21545144, ECO:0000305|PubMed:21604715 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 320 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:11812140, ECO:0000269|PubMed:15381761, ECO:0000269|PubMed:21545144 source Swiss-Prot : SWS_FT_FI4 23) chain A residue 247 type SITE sequence T description Activates the nucleophilic water => ECO:0000305|PubMed:21545144, ECO:0000305|PubMed:21604715 source Swiss-Prot : SWS_FT_FI5 24) 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 25) chain A residue 64 type BINDING sequence L description BINDING => ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|Ref.14 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 215 type BINDING sequence C description BINDING => ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|Ref.14 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 314 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|Ref.14 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 157 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11812140, ECO:0000269|PubMed:15381761, ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715 source Swiss-Prot : SWS_FT_FI3

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