4X3F
Crystal structure of the intracellular domain of the M. tuberculosis Ser/Thr kinase PknA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0004672 | molecular_function | protein kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
C | 0004672 | molecular_function | protein kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006468 | biological_process | protein phosphorylation |
Functional Information from PROSITE/UniProt
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LvHrDVKpgNILI |
Chain | Residue | Details |
C | LEU137-ILE149 | |
B | LEU137-ILE149 | |
A | LEU137-ILE149 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
Chain | Residue | Details |
C | ASP141 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
C | ILE19 | |
C | LYS42 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:25586004 |
Chain | Residue | Details |
C | THR8 | |
C | THR252 | |
C | THR302 | |
C | THR313 | |
C | THR21 | |
C | THR64 | |
C | THR65 | |
C | THR90 | |
C | THR125 | |
C | THR152 | |
C | THR158 | |
C | TPO224 |
site_id | SWS_FT_FI4 |
Number of Residues | 7 |
Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:25586004 |
Chain | Residue | Details |
C | SER10 | |
C | SER46 | |
C | SER75 | |
C | SER105 | |
C | SER198 | |
C | SER263 | |
C | SER309 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:25665034 |
Chain | Residue | Details |
C | THR172 | |
C | THR174 | |
C | THR180 |