eF-site ID 1o3s-A PDB Code 1o3s Chain A click to enlarge Title PROTEIN-DNA RECOGNITION AND DNA DEFORMATION REVEALED IN CRYSTAL STRUCTURES OF CAP-DNA COMPLEXES Classification GENE REGULATION/DNA Compound 5'-D(*AP*AP*AP*AP*AP*TP*GP*CP*GP*AP*T)-3' Source Escherichia coli (strain K12) (1O3S) Sequence A:  DPTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSV AVLIKDEEGKEMILSYLNQGDFIGELGLFEEGQERSAWVR AKTACEVAEISYKKFRQLIQVNPDILMRLSAQMARRLQVT SEKVGNLAFLDVTGRIAQTLLNLAKQPDAMTHPDGMQIKI TRQEIGQIVGCSRDTVGRILKMLEDQNLISAHGKTIVVYG Description Functional site 1) chain A residue 49 type sequence V description BINDING SITE FOR RESIDUE CMP A 1 source : AC1 2) chain A residue 61 type sequence L description BINDING SITE FOR RESIDUE CMP A 1 source : AC1 3) chain A residue 70 type sequence I description BINDING SITE FOR RESIDUE CMP A 1 source : AC1 4) chain A residue 71 type sequence G description BINDING SITE FOR RESIDUE CMP A 1 source : AC1 5) chain A residue 72 type sequence E description BINDING SITE FOR RESIDUE CMP A 1 source : AC1 6) chain A residue 73 type sequence L description BINDING SITE FOR RESIDUE CMP A 1 source : AC1 7) chain A residue 82 type sequence R description BINDING SITE FOR RESIDUE CMP A 1 source : AC1 8) chain A residue 83 type sequence S description BINDING SITE FOR RESIDUE CMP A 1 source : AC1 9) chain A residue 123 type sequence R description BINDING SITE FOR RESIDUE CMP A 1 source : AC1 10) chain A residue 127 type sequence T description BINDING SITE FOR RESIDUE CMP A 1 source : AC1 11) chain A residue 128 type sequence S description BINDING SITE FOR RESIDUE CMP A 1 source : AC1 12) chain A residue 57 type sequence K description BINDING SITE FOR RESIDUE CMP A 2 source : AC2 13) chain A residue 58 type sequence E description BINDING SITE FOR RESIDUE CMP A 2 source : AC2 14) chain A residue 135 type sequence A description BINDING SITE FOR RESIDUE CMP A 2 source : AC2 15) chain A residue 136 type sequence F description BINDING SITE FOR RESIDUE CMP A 2 source : AC2 16) chain A residue 170 type sequence Q description BINDING SITE FOR RESIDUE CMP A 2 source : AC2 17) chain A residue 173 type sequence G description BINDING SITE FOR RESIDUE CMP A 2 source : AC2 18) chain A residue 174 type sequence Q description BINDING SITE FOR RESIDUE CMP A 2 source : AC2 19) chain A residue 178 type sequence C description BINDING SITE FOR RESIDUE CMP A 2 source : AC2 20) chain A residue 179 type sequence S description BINDING SITE FOR RESIDUE CMP A 2 source : AC2 21) chain A residue 180 type sequence R description BINDING SITE FOR RESIDUE CMP A 2 source : AC2 22) chain A residue 167-190 type prosite sequence ITRQEIGQIVGCSRDTVGRILKML description HTH_CRP_1 Crp-type HTH domain signature. ITRqeIGqIVGcSrdTv.GRiLkmL source prosite : PS00042 23) chain A residue 29-45 type prosite sequence LIHQGEKAETLYYIVKG description CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. LIhQGEkAEtLYYIvkG source prosite : PS00888 24) chain A residue 70-88 type prosite sequence IGELGLFEEGQERSAWVRA description CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. IGElGLfeegqe.....RSAwVrA source prosite : PS00889 25) chain A residue 179-185 type DNA_BIND sequence SRDTVGR description H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00387 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 56 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 71 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 82 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 127 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 135 type BINDING sequence A description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 170 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802 source Swiss-Prot : SWS_FT_FI2 32) chain A residue 96 type SITE sequence E description Activating region 2 (AR2); probably contacts the N-terminus of RpoA => ECO:0000269|PubMed:8978616 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 101 type SITE sequence K description Activating region 2 (AR2); probably contacts the N-terminus of RpoA => ECO:0000269|PubMed:15520470, ECO:0000269|PubMed:8978616 source Swiss-Prot : SWS_FT_FI4 34) chain A residue 100 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI5

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