3DNT
structures of MDT proteins
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0000976 | molecular_function | transcription cis-regulatory region binding |
| A | 0001217 | molecular_function | DNA-binding transcription repressor activity |
| A | 0003677 | molecular_function | DNA binding |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0022611 | biological_process | dormancy process |
| A | 0032993 | cellular_component | protein-DNA complex |
| A | 0036289 | biological_process | peptidyl-serine autophosphorylation |
| A | 0040008 | biological_process | regulation of growth |
| A | 0043565 | molecular_function | sequence-specific DNA binding |
| A | 0044010 | biological_process | single-species biofilm formation |
| A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0106310 | molecular_function | protein serine kinase activity |
| A | 0110001 | cellular_component | toxin-antitoxin complex |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0000976 | molecular_function | transcription cis-regulatory region binding |
| B | 0001217 | molecular_function | DNA-binding transcription repressor activity |
| B | 0003677 | molecular_function | DNA binding |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0022611 | biological_process | dormancy process |
| B | 0032993 | cellular_component | protein-DNA complex |
| B | 0036289 | biological_process | peptidyl-serine autophosphorylation |
| B | 0040008 | biological_process | regulation of growth |
| B | 0043565 | molecular_function | sequence-specific DNA binding |
| B | 0044010 | biological_process | single-species biofilm formation |
| B | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0106310 | molecular_function | protein serine kinase activity |
| B | 0110001 | cellular_component | toxin-antitoxin complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE ATP A 500 |
| Chain | Residue |
| A | VAL98 |
| A | VAL233 |
| A | GLU234 |
| A | ARG235 |
| A | PHE236 |
| A | ASP237 |
| A | GLN252 |
| A | HIS311 |
| A | LYS313 |
| A | ASN314 |
| A | TYR331 |
| A | ALA152 |
| A | ASP332 |
| A | MG441 |
| A | MG442 |
| A | HOH860 |
| A | HOH861 |
| A | HOH867 |
| A | HOH932 |
| A | HOH1063 |
| A | GLY153 |
| A | ALA154 |
| A | GLN155 |
| A | LYS157 |
| A | ILE179 |
| A | LYS181 |
| A | PRO218 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 441 |
| Chain | Residue |
| A | ASN314 |
| A | ASP332 |
| A | ATP500 |
| A | HOH860 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 442 |
| Chain | Residue |
| A | GLN309 |
| A | ASP332 |
| A | ATP500 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 833 |
| Chain | Residue |
| A | ALA358 |
| A | SER359 |
| A | LYS363 |
| A | ARG372 |
| A | HIS373 |
| A | HOH1014 |
| A | HOH1201 |
| site_id | AC5 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE ATP B 501 |
| Chain | Residue |
| B | ASP67 |
| B | VAL98 |
| B | ALA152 |
| B | GLY153 |
| B | ALA154 |
| B | GLN155 |
| B | LYS157 |
| B | ILE179 |
| B | LYS181 |
| B | VAL233 |
| B | GLU234 |
| B | ARG235 |
| B | PHE236 |
| B | ASP237 |
| B | GLN252 |
| B | HIS311 |
| B | LYS313 |
| B | ASN314 |
| B | TYR331 |
| B | ASP332 |
| B | MG441 |
| B | MG442 |
| B | HOH835 |
| B | HOH837 |
| B | HOH842 |
| B | HOH858 |
| B | HOH861 |
| B | HOH1011 |
| B | HOH1145 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 441 |
| Chain | Residue |
| B | ASP332 |
| B | ATP501 |
| B | HOH1058 |
| B | HOH1165 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 442 |
| Chain | Residue |
| B | ASN314 |
| B | ASP332 |
| B | ATP501 |
| B | HOH835 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 834 |
| Chain | Residue |
| B | ALA358 |
| B | SER359 |
| B | LYS363 |
| B | ARG372 |
| B | HIS373 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | DNA binding: {"evidences":[{"source":"PubMed","id":"19150849","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17041039","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22999936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3DNT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FBR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HZI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TPT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"17041039","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22999936","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
