eF-site ID 1k6w-A PDB Code 1k6w Chain A click to enlarge Title The Structure of Escherichia coli Cytosine Deaminase Classification HYDROLASE Compound Cytosine Deaminase Source null (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 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 247 type SITE sequence T description Activates the nucleophilic water => ECO:0000305|PubMed:21545144, ECO:0000305|PubMed:21604715 source Swiss-Prot : SWS_FT_FI5 6) chain A residue 62 type catalytic sequence I description 710 source MCSA : MCSA1 7) chain A residue 64 type catalytic sequence L description 710 source MCSA : MCSA1 8) chain A residue 157 type catalytic sequence E description 710 source MCSA : MCSA1 9) chain A residue 215 type catalytic sequence C description 710 source MCSA : MCSA1 10) chain A residue 218 type catalytic sequence I description 710 source MCSA : MCSA1 11) chain A residue 314 type catalytic sequence D description 710 source MCSA : MCSA1 12) 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 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 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 15) 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 16) 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 17) 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 18) 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

Display surface Download Links