3D-footprint cannot reliably estimate the specificity of 'Nucleic acid-binding proteins', as they bind to single-stranded DNA and thus accumulate more base contacts.


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updated Wed Sep 11 00:45:58 2024
structure nameCRYO-EM STRUCTURE OF ECMRR-RNAP-PROMOTER OPEN COMPLEX (ECMRR-RPO)
sourceESCHERICHIA COLI O157:H7
experimentNMR
structural superfamilycAMP-binding domain-like;"Winged helix" DNA-binding domain;P-loop containing nucleoside triphosphate hydrolases;Putative DNA-binding domain;beta and beta-prime subunits of DNA dependent RNA-polymerase;Nucleic acid-binding proteins;Rho N-terminal domain-like;Probable bacterial effector-binding domain;Homeodomain-like;Insert subdomain of RNA polymerase alpha subunit;RBP11-like subunits of RNA polymerase;C-terminal domain of RNA polymerase alpha subunit;lambda repressor-like DNA-binding domains;CheY-like;C-terminal effector domain of the bipartite response regulators;
reference complex3iyd_H 5nss_G 6ldi_G 6vu3_A 6vz3_A 6xas_B 6xh7_H 6xl5_H 7vwz_G 7w5x_A 8igr_C 8jo2_H 8u3b_G 8upo_A
links to other resourcesNAKB PDBSum PDIdb DNAproDB
protein sequence