3FBR
structure of HipA-amppnp-peptide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0022611 | biological_process | dormancy process |
| A | 0032993 | cellular_component | protein-DNA complex |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ACP A 500 |
| Chain | Residue |
| A | VAL98 |
| A | PHE236 |
| A | GLN252 |
| A | GLN309 |
| A | HIS311 |
| A | LYS313 |
| A | ASN314 |
| A | TYR331 |
| A | ASP332 |
| A | HOH439 |
| A | GLY153 |
| A | ALA154 |
| A | GLN155 |
| A | LYS157 |
| A | LYS181 |
| A | PRO218 |
| A | VAL233 |
| A | ARG235 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | DNA_BIND: DNA_BIND => ECO:0000269|PubMed:19150849 |
| Chain | Residue | Details |
| A | LYS379-ARG382 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:17041039 |
| Chain | Residue | Details |
| A | GLN309 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22999936, ECO:0007744|PDB:3DNT, ECO:0007744|PDB:3FBR, ECO:0007744|PDB:3HZI, ECO:0007744|PDB:3TPT |
| Chain | Residue | Details |
| A | GLU234 | |
| A | HIS311 | |
| A | TYR331 | |
| A | ALA152 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22999936, ECO:0007744|PDB:3DNT, ECO:0007744|PDB:3HZI, ECO:0007744|PDB:3TPT |
| Chain | Residue | Details |
| A | LYS181 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:17041039, ECO:0000269|PubMed:22999936 |
| Chain | Residue | Details |
| A | SER150 |
