3TPD
Structure of pHipA, monoclinic form
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 | 0006338 | biological_process | chromatin remodeling |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0016310 | biological_process | phosphorylation |
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 | 0044024 | molecular_function | histone H2AS1 kinase activity |
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 | 6 |
Details | BINDING SITE FOR RESIDUE CL A 441 |
Chain | Residue |
A | GLY164 |
A | ASN165 |
A | LYS363 |
A | THR364 |
A | ALA365 |
A | HOH549 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 A 833 |
Chain | Residue |
A | ARG372 |
A | HIS373 |
A | HOH506 |
A | HOH598 |
A | ALA358 |
A | SER359 |
A | LYS363 |
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 | ASP309 |
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 | ALA152 | |
A | GLU234 | |
A | HIS311 | |
A | TYR331 |
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 |