eF-site ID 5dqz-ABCDEF PDB Code 5dqz Chain A, B, C, D, E, F click to enlarge Title Crystal Structure of Cas-DNA-PAM complex Classification HYDROLASE/DNA Compound CRISPR-associated endonuclease Cas1 Source Escherichia coli (strain K12) (CAS2_ECOLI) Sequence A:  VSMIFLQYGQIDVIDGAFVLIDKTGIRTHIPVGSVACIML EPGTRVSHAAVRLAAQVGTLLVWVGEAGVRVYASGQPGGA RSDKLLYQAKLALDEDLRLKVVRKMFELRFGEPAPARRSV EQLRGIEGSRVRATYALLAKQYGVTWNGRRYDPKDWEKGD TINQCISAATSCLYGVTEAAILAAGYAPAIGFVHTGKPLS FVYDIADIIKFDTVVPKAFEIARRNPGEPDREVRLACRDI FRSSKTLAKLIPLIEDVLAAGEIQPPA B:  TWLPLNPIPLKDRVSMIFLQYGQIDVIDGAFVLIDKTGIR THIPVGSVACIMLEPGTRVSHAAVRLAAQVGTLLVWVGEA GVRVYASGQPGGARSDKLLYQAKLALDEDLRLKVVRKMFE LRFGEPAPARRSVEQLRGIEGSRVRATYALLAKQYGVTWN GRRYDPKKGDTINQCISAATSCLYGVTEAAILAAGYAPAI GFVHTGKPLSFVYDIADIIKFDTVVPKAFEIARRNPGEPD REVRLACRDIFRSSKTLAKLIPLIEDVLAAGEIQPPAPPE DAQPVAIPLPVSLGDAGHRSS C:  TWLPLNPIPLKDRVSMIFLQYGQIDVIDGAFVLIDKTGIR THIPVGSVACIMLEPGTRVSHAAVRLAAQVGTLLVWVGEA GVRVYASGQPGGARSDKLLYQAKLALDEDLRLKVVRKMFE LRFGEPAPARRSVEQLRGIEGSRVRATYALLAKQYGVTWN GRRYDPKGDTINQCISAATSCLYGVTEAAILAAGYAPAIG FVHTGKPLSFVYDIADIIKFDTVVPKAFEIARRNPGEPDR EVRLACRDIFRSSKTLAKLIPLIEDVLAAGEIQPPAPPED AQPVAIPLPVSLGDAGHRSS D:  VSMIFLQYGQIDVIDGAFVLIDKTGIRTHIPVGSVACIML EPGTRVSHAAVRLAAQVGTLLVWVGEAGVRVYASGQPGGA RSDKLLYQAKLALDEDLRLKVVRKMFELRFGEPAPARRSV EQLRGIEGSRVRATYALLAKQYGVTWNGRRYDPKDWEKGD TINQCISAATSCLYGVTEAAILAAGYAPAIGFVHTGKPLS FVYDIADIIKFDTVVPKAFEIARRNPGEPDREVRLACRDI FRSSKTLAKLIPLIEDVLAAGEIQPPA E:  MSMLVVVTENVPPRLRGRLAIWLLEVRAGVYVGDVSAKIR EMIWEQIAGLAEEGNVVMAWATNTETGFEFQTFGLNRRTP VDLDGLRLVSFLPV F:  MSMLVVVTENVPPRLRGRLAIWLLEVRAGVYVGDVSAKIR EMIWEQIAGLAEEGNVVMAWATNTETGFEFQTFGLNRRTP VDLDGLRLVSFLPV Description Functional site 1) chain C residue 141 type sequence E description binding site for residue MG C 401 source : AC1 2) chain C residue 208 type sequence H description binding site for residue MG C 401 source : AC1 3) chain C residue 221 type sequence D description binding site for residue MG C 401 source : AC1 4) chain B residue 141 type sequence E description binding site for residue MG B 401 source : AC2 5) chain B residue 208 type sequence H description binding site for residue MG B 401 source : AC2 6) chain B residue 221 type sequence D description binding site for residue MG B 401 source : AC2 7) chain D residue 141 type BINDING sequence E description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5 source Swiss-Prot : SWS_FT_FI1 8) chain D residue 221 type BINDING sequence D description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5 source Swiss-Prot : SWS_FT_FI1 9) chain C residue 141 type BINDING sequence E description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5 source Swiss-Prot : SWS_FT_FI1 10) chain C residue 221 type BINDING sequence D description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5 source Swiss-Prot : SWS_FT_FI1 11) chain A residue 141 type BINDING sequence E description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5 source Swiss-Prot : SWS_FT_FI1 12) chain A residue 221 type BINDING sequence D description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5 source Swiss-Prot : SWS_FT_FI1 13) chain B residue 141 type BINDING sequence E description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5 source Swiss-Prot : SWS_FT_FI1 14) chain B residue 221 type BINDING sequence D description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5 source Swiss-Prot : SWS_FT_FI1 15) chain D residue 208 type BINDING sequence H description BINDING => ECO:0000305|PubMed:26503043 source Swiss-Prot : SWS_FT_FI2 16) chain C residue 208 type BINDING sequence H description BINDING => ECO:0000305|PubMed:26503043 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 208 type BINDING sequence H description BINDING => ECO:0000305|PubMed:26503043 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 208 type BINDING sequence H description BINDING => ECO:0000305|PubMed:26503043 source Swiss-Prot : SWS_FT_FI2

Display surface Download Links