eF-site ID 2y7h-ABCDE PDB Code 2y7h Chain A, B, C, D, E click to enlarge Title Atomic model of the DNA-bound methylase complex from the Type I restriction-modification enzyme EcoKI (M2S1). Based on fitting into EM map 1534. Classification TRANSFERASE/DNA Compound TYPE-1 RESTRICTION ENZYME ECOKI SPECIFICITY PROTEIN Source ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; Sequence A:  MSAGKLPEGWVIAPVSTVTTLIRGVTYKKEQAINYLKDDY LPLIRANNIQNGKFDTTDLVFVPKNLVKESQKISPEDIVI AMSSGSKSVVGKSAHQHLPFECSFGAFCGVLRPEKLIFSG FIAHFTKSSLYRNKISSLSAGANINNIKPASFDLINIPIP PLAEQKIIAEKLDTLLAQVDSTKARFEQIPQILKRFRQAV LGGAVNGKLTEKWRNFEPQHSVFKKLNFESILTELRNGLS SKPNESGVGHPILRISSVRAGHVDQNDIRFLECSESELNR HKLQDGDLLFTRYNGSLEFVGVCGLLKKLQHQNLLYPDKL IRARLTKDALPEYIEIFFSSPSARNAMMNCVKTTSGQKGI SGKDIKSQVVLLPPVKEQAEIVRRVEQLFAYADTIEKQVN NALARVNNLTQSILAKAFRGELTAQWRAENPDLISGENSA AALLEKIKAERAASGGKKASRKKS B:  MNNNDLVAKLWKLCDNLRDGGVSYQNYVNELASLLFLKMC KETGQEAEYLPEGYRWDDLKSRIGQEQLQFYRKMLVHLGE DDKKLVQAVFHNVSTTITEPKQITALVSNMDSLDWYNGAH GKSRDDFGDMYEGLLQKNANETKSGAGQYFTPRPLIKTII HLLKPQPREVVQDPAAGTAGFLIEADRYVKSQTNDLDDLD GDTQDFQIHRAFIGLELVPGTRRLALMNCLLHDIEGNLDH GGAIRLGNTLGSDGENLPKAHIVATNPPFGSAAGTNITRT FVHPTSNKQLCFMQHIIETLHPGGRAAVVVPDNVLFEGGK GTDIRRDLMDKCHLHTILRLPTGIFYAQGVKTNVLFFTKG TVANPNQDKNCTDDVWVYDLRTNMPSFGKRTPFTDEHLQP FERVYGEDPHGLSPRTEGEWSFNAEETEVADSEENKNTDQ HLATSRWRKFSREWIRTAKSDSLDISWLKDKDSIDADSLP EPDVLAAEAMGELVQALSELDALMRELGASDEADLQRQLL EEAFGGVKE C:  MNNNDLVAKLWKLCDNLRDGGVSYQNYVNELASLLFLKMC KETGQEAEYLPEGYRWDDLKSRIGQEQLQFYRKMLVHLGE DDKKLVQAVFHNVSTTITEPKQITALVSNMDSLDWYNGAH GKSRDDFGDMYEGLLQKNANETKSGAGQYFTPRPLIKTII HLLKPQPREVVQDPAAGTAGFLIEADRYVKSQTNDLDDLD GDTQDFQIHRAFIGLELVPGTRRLALMNCLLHDIEGNLDH GGAIRLGNTLGSDGENLPKAHIVATNPPFGSAAGTNITRT FVHPTSNKQLCFMQHIIETLHPGGRAAVVVPDNVLFEGGK GTDIRRDLMDKCHLHTILRLPTGIFYAQGVKTNVLFFTKG TVANPNQDKNCTDDVWVYDLRTNMPSFGKRTPFTDEHLQP FERVYGEDPHGLSPRTEGEWSFNAEETEVADSEENKNTDQ HLATSRWRKFSREWIRTAKSDSLDISWLKDKDSIDADSLP EPDVLAAEAMGELVQALSELDALMRELGASDEADLQRQLL EEAFGGVKE D:  GTTCAACGTCGACGTGCAAC E:  GTTGCACGTCGACGTTGAAC Description (1)  TYPE-1 RESTRICTION ENZYME ECOKI SPECIFICITY PROTEIN (E.C.3.1.21.3), TYPE I RESTRICTION ENZYME ECOKI M PROTEIN (E.C.3.1.21.3, 2.1.1.72) Functional site 1) chain B residue 148 type sequence Q description BINDING SITE FOR RESIDUE SAM B 530 source : AC1 2) chain B residue 149 type sequence Y description BINDING SITE FOR RESIDUE SAM B 530 source : AC1 3) chain B residue 151 type sequence T description BINDING SITE FOR RESIDUE SAM B 530 source : AC1 4) chain B residue 175 type sequence A description BINDING SITE FOR RESIDUE SAM B 530 source : AC1 5) chain B residue 177 type sequence G description BINDING SITE FOR RESIDUE SAM B 530 source : AC1 6) chain B residue 178 type sequence T description BINDING SITE FOR RESIDUE SAM B 530 source : AC1 7) chain B residue 180 type sequence G description BINDING SITE FOR RESIDUE SAM B 530 source : AC1 8) chain B residue 181 type sequence F description BINDING SITE FOR RESIDUE SAM B 530 source : AC1 9) chain B residue 216 type sequence E description BINDING SITE FOR RESIDUE SAM B 530 source : AC1 10) chain B residue 248 type sequence N description BINDING SITE FOR RESIDUE SAM B 530 source : AC1 11) chain B residue 249 type sequence T description BINDING SITE FOR RESIDUE SAM B 530 source : AC1 12) chain B residue 266 type sequence N description BINDING SITE FOR RESIDUE SAM B 530 source : AC1 13) chain B residue 268 type sequence P description BINDING SITE FOR RESIDUE SAM B 530 source : AC1 14) chain B residue 275 type sequence T description BINDING SITE FOR RESIDUE SAM B 530 source : AC1 15) chain B residue 292 type sequence F description BINDING SITE FOR RESIDUE SAM B 530 source : AC1 16) chain D residue 6 type sequence A description BINDING SITE FOR RESIDUE SAM B 530 source : AC1 17) chain C residue 148 type sequence Q description BINDING SITE FOR RESIDUE SAM C 530 source : AC2 18) chain C residue 149 type sequence Y description BINDING SITE FOR RESIDUE SAM C 530 source : AC2 19) chain C residue 151 type sequence T description BINDING SITE FOR RESIDUE SAM C 530 source : AC2 20) chain C residue 175 type sequence A description BINDING SITE FOR RESIDUE SAM C 530 source : AC2 21) chain C residue 177 type sequence G description BINDING SITE FOR RESIDUE SAM C 530 source : AC2 22) chain C residue 178 type sequence T description BINDING SITE FOR RESIDUE SAM C 530 source : AC2 23) chain C residue 180 type sequence G description BINDING SITE FOR RESIDUE SAM C 530 source : AC2 24) chain C residue 181 type sequence F description BINDING SITE FOR RESIDUE SAM C 530 source : AC2 25) chain C residue 216 type sequence E description BINDING SITE FOR RESIDUE SAM C 530 source : AC2 26) chain C residue 248 type sequence N description BINDING SITE FOR RESIDUE SAM C 530 source : AC2 27) chain C residue 249 type sequence T description BINDING SITE FOR RESIDUE SAM C 530 source : AC2 28) chain C residue 266 type sequence N description BINDING SITE FOR RESIDUE SAM C 530 source : AC2 29) chain C residue 268 type sequence P description BINDING SITE FOR RESIDUE SAM C 530 source : AC2 30) chain C residue 275 type sequence T description BINDING SITE FOR RESIDUE SAM C 530 source : AC2 31) chain E residue 6 type sequence A description BINDING SITE FOR RESIDUE SAM C 530 source : AC2 32) chain B residue 263-269 type prosite sequence VATNPPF description N6_MTASE N-6 Adenine-specific DNA methylases signature. VATNPPF source prosite : PS00092 33) chain B residue 148 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q89Z59 source Swiss-Prot : SWS_FT_FI1 34) chain B residue 178 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q89Z59 source Swiss-Prot : SWS_FT_FI1 35) chain B residue 216 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q89Z59 source Swiss-Prot : SWS_FT_FI1 36) chain C residue 148 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q89Z59 source Swiss-Prot : SWS_FT_FI1 37) chain C residue 178 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q89Z59 source Swiss-Prot : SWS_FT_FI1 38) chain C residue 216 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q89Z59 source Swiss-Prot : SWS_FT_FI1

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