eF-site ID 3o7u-A PDB Code 3o7u Chain A click to enlarge Title Crystal structure of Cytosine Deaminase from Escherichia Coli complexed with zinc and phosphono-cytosine Classification HYDROLASE/HYDROLASE INHIBITOR Compound Cytosine deaminase Source Escherichia coli (Q53ZC8_ECOLX) Sequence A:  ALQTIINARLPGEEGLWQIHLQDGKISAIDAQSGVMPITE NSLDAEQGLVIPPFVEPHIHLDTTQTAGQPNWNQSGTLFE GIERWAERKALLTHDDVKQRAWQTLKWQIANGIQHVRTHV DVSDATLTALKAMLEVKQEVAPWIDLQIVAFPQEGILSYP NGEALLEEALRLGADVVGAIPHFEFTREYGVESLHKTFAL AQKYDRLIDVHCDEIDDEQSRFVETVAALAHHEGMGARVT ASHTTAMHSYNGAYTSRLFRLLKMSGINFVANPLVNIHLQ GRFDTYPKRRGITRVKEMLESGINVCFGHDDVFDPWYPLG TANMLQVLHMGLHVCQLMGYGQINDGLNLITHHSARTLNL QDYGIAAGNSANLIILPAENGFDALRRQVPVRYSVRGGKV IASTQPAQTTVYLEQPEAIDYK Description Functional site 1) chain A residue 102 type sequence Q description BINDING SITE FOR RESIDUE PXN A 427 source : AC1 2) chain A residue 105 type sequence W description BINDING SITE FOR RESIDUE PXN A 427 source : AC1 3) chain A residue 106 type sequence Q description BINDING SITE FOR RESIDUE PXN A 427 source : AC1 4) chain A residue 109 type sequence K description BINDING SITE FOR RESIDUE PXN A 427 source : AC1 5) chain A residue 417 type sequence E description BINDING SITE FOR RESIDUE PXN A 427 source : AC1 6) chain A residue 61 type sequence H description BINDING SITE FOR RESIDUE ZN A 428 source : AC2 7) chain A residue 63 type sequence H description BINDING SITE FOR RESIDUE ZN A 428 source : AC2 8) chain A residue 214 type sequence H description BINDING SITE FOR RESIDUE ZN A 428 source : AC2 9) chain A residue 313 type sequence D description BINDING SITE FOR RESIDUE ZN A 428 source : AC2 10) chain A residue 97 type sequence H description BINDING SITE FOR RESIDUE ZN A 429 source : AC3 11) chain A residue 97 type sequence H description BINDING SITE FOR RESIDUE ZN A 429 source : AC3 12) chain A residue 138 type sequence E description BINDING SITE FOR RESIDUE ZN A 429 source : AC3 13) chain A residue 138 type sequence E description BINDING SITE FOR RESIDUE ZN A 429 source : AC3 14) chain A residue 61 type sequence H description BINDING SITE FOR RESIDUE O7U A 430 source : AC4 15) chain A residue 63 type sequence H description BINDING SITE FOR RESIDUE O7U A 430 source : AC4 16) chain A residue 81 type sequence L description BINDING SITE FOR RESIDUE O7U A 430 source : AC4 17) chain A residue 156 type sequence Q description BINDING SITE FOR RESIDUE O7U A 430 source : AC4 18) chain A residue 214 type sequence H description BINDING SITE FOR RESIDUE O7U A 430 source : AC4 19) chain A residue 217 type sequence E description BINDING SITE FOR RESIDUE O7U A 430 source : AC4 20) chain A residue 246 type sequence H description BINDING SITE FOR RESIDUE O7U A 430 source : AC4 21) chain A residue 313 type sequence D description BINDING SITE FOR RESIDUE O7U A 430 source : AC4 22) chain A residue 314 type sequence D description BINDING SITE FOR RESIDUE O7U A 430 source : AC4 23) chain A residue 319 type sequence W description BINDING SITE FOR RESIDUE O7U A 430 source : AC4 24) chain A residue 160 type sequence L description BINDING SITE FOR RESIDUE GOL A 431 source : AC5 25) chain A residue 163 type sequence P description BINDING SITE FOR RESIDUE GOL A 431 source : AC5 26) chain A residue 188 type sequence F description BINDING SITE FOR RESIDUE GOL A 431 source : AC5 27) chain A residue 234 type sequence H description BINDING SITE FOR RESIDUE GOL A 431 source : AC5 28) chain A residue 235 type sequence H description BINDING SITE FOR RESIDUE GOL A 431 source : AC5 29) chain A residue 390 type sequence R description BINDING SITE FOR RESIDUE GOL A 432 source : AC6 30) chain A residue 424 type sequence Y description BINDING SITE FOR RESIDUE GOL A 432 source : AC6 31) chain A residue 345 type sequence Q description BINDING SITE FOR RESIDUE GOL A 433 source : AC7 32) chain A residue 348 type sequence D description BINDING SITE FOR RESIDUE GOL A 433 source : AC7 33) chain A residue 351 type sequence N description BINDING SITE FOR RESIDUE GOL A 433 source : AC7 34) chain A residue 352 type sequence L description BINDING SITE FOR RESIDUE GOL A 433 source : AC7 35) chain A residue 258 type sequence T description BINDING SITE FOR RESIDUE GOL A 434 source : AC8 36) chain A residue 259 type sequence S description BINDING SITE FOR RESIDUE GOL A 434 source : AC8 37) chain A residue 300 type sequence E description BINDING SITE FOR RESIDUE GOL A 434 source : AC8 38) chain A residue 205 type sequence Q description BINDING SITE FOR RESIDUE GOL A 435 source : AC9 39) chain A residue 208 type sequence D description BINDING SITE FOR RESIDUE GOL A 435 source : AC9 40) chain A residue 49 type sequence E description BINDING SITE FOR RESIDUE GOL A 436 source : BC1 41) chain A residue 50 type sequence Q description BINDING SITE FOR RESIDUE GOL A 436 source : BC1 42) chain A residue 380 type sequence P description BINDING SITE FOR RESIDUE GOL A 436 source : BC1 43) chain A residue 381 type sequence A description BINDING SITE FOR RESIDUE GOL A 436 source : BC1 44) chain A residue 382 type sequence E description BINDING SITE FOR RESIDUE GOL A 436 source : BC1 45) chain A residue 425 type sequence K description BINDING SITE FOR RESIDUE GOL A 436 source : BC1 46) chain A residue 72 type sequence Q description BINDING SITE FOR RESIDUE PEG A 438 source : BC2 47) chain A residue 73 type sequence P description BINDING SITE FOR RESIDUE PEG A 438 source : BC2 48) chain A residue 94 type sequence L description BINDING SITE FOR RESIDUE PEG A 438 source : BC2 49) chain A residue 61 type catalytic sequence H description 710 source MCSA : MCSA1 50) chain A residue 63 type catalytic sequence H description 710 source MCSA : MCSA1 51) chain A residue 156 type catalytic sequence Q description 710 source MCSA : MCSA1 52) chain A residue 214 type catalytic sequence H description 710 source MCSA : MCSA1 53) chain A residue 217 type catalytic sequence E description 710 source MCSA : MCSA1 54) chain A residue 313 type catalytic sequence D description 710 source MCSA : MCSA1 55) chain A residue 217 type ACT_SITE sequence E description Proton donor => ECO:0000305|PubMed:11812140, ECO:0000305|PubMed:21545144, ECO:0000305|PubMed:21604715 source Swiss-Prot : SWS_FT_FI1 56) chain A residue 61 type BINDING sequence H description BINDING => ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|Ref.14 source Swiss-Prot : SWS_FT_FI2 57) chain A residue 63 type BINDING sequence H description BINDING => ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|Ref.14 source Swiss-Prot : SWS_FT_FI2 58) chain A residue 214 type BINDING sequence H description BINDING => ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|Ref.14 source Swiss-Prot : SWS_FT_FI2 59) chain A residue 313 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|Ref.14 source Swiss-Prot : SWS_FT_FI2 60) chain A residue 156 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:11812140, ECO:0000269|PubMed:15381761, ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715 source Swiss-Prot : SWS_FT_FI3 61) chain A residue 319 type BINDING sequence W description BINDING => ECO:0000269|PubMed:11812140, ECO:0000269|PubMed:15381761, ECO:0000269|PubMed:21545144 source Swiss-Prot : SWS_FT_FI4 62) chain A residue 246 type SITE sequence H description Activates the nucleophilic water => ECO:0000305|PubMed:21545144, ECO:0000305|PubMed:21604715 source Swiss-Prot : SWS_FT_FI5

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