2PZI
Crystal Structure of Protein kinase PknG from Mycobacterium tuberculosis in Complex with Tetrahydrobenzothiophene AX20017
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006468 | biological_process | protein phosphorylation |
A | 0006538 | biological_process | glutamate catabolic process |
A | 0006543 | biological_process | glutamine catabolic process |
A | 0030682 | biological_process | symbiont-mediated perturbation of host defenses |
A | 0042783 | biological_process | evasion of host immune response |
A | 0042802 | molecular_function | identical protein binding |
A | 0046677 | biological_process | response to antibiotic |
A | 0046777 | biological_process | protein autophosphorylation |
A | 0052027 | biological_process | symbiont-mediated perturbation of host signal transduction pathway |
A | 0052170 | biological_process | symbiont-mediated suppression of host innate immune response |
A | 0106310 | molecular_function | protein serine kinase activity |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004674 | molecular_function | protein serine/threonine kinase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
B | 0006468 | biological_process | protein phosphorylation |
B | 0006538 | biological_process | glutamate catabolic process |
B | 0006543 | biological_process | glutamine catabolic process |
B | 0030682 | biological_process | symbiont-mediated perturbation of host defenses |
B | 0042783 | biological_process | evasion of host immune response |
B | 0042802 | molecular_function | identical protein binding |
B | 0046677 | biological_process | response to antibiotic |
B | 0046777 | biological_process | protein autophosphorylation |
B | 0052027 | biological_process | symbiont-mediated perturbation of host signal transduction pathway |
B | 0052170 | biological_process | symbiont-mediated suppression of host innate immune response |
B | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 751 |
Chain | Residue |
A | ALA148 |
A | GLU218 |
A | HIS219 |
A | HOH880 |
B | ARG714 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD A 752 |
Chain | Residue |
A | CYS105 |
A | CYS108 |
A | CYS128 |
A | CYS131 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD B 751 |
Chain | Residue |
B | CYS105 |
B | CYS108 |
B | CYS128 |
B | CYS131 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE AXX B 752 |
Chain | Residue |
B | ILE157 |
B | VAL179 |
B | MET232 |
B | GLU233 |
B | TYR234 |
B | VAL235 |
B | GLY237 |
B | ILE292 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE AXX A 753 |
Chain | Residue |
A | ALA91 |
A | MET232 |
A | GLU233 |
A | TYR234 |
A | VAL235 |
A | ILE292 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 754 |
Chain | Residue |
A | PRO417 |
A | SER418 |
A | VAL602 |
A | HOH805 |
B | GLN478 |
B | SER482 |
B | HOH863 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL B 753 |
Chain | Residue |
B | ARG397 |
B | GLY410 |
B | SER412 |
B | GLY568 |
B | GLU569 |
B | LEU570 |
B | HOH764 |
B | HOH770 |
B | HOH859 |
B | HOH880 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 755 |
Chain | Residue |
A | GLN475 |
A | PRO476 |
A | VAL477 |
A | GLN478 |
B | SER420 |
B | THR421 |
B | HIS635 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 756 |
Chain | Residue |
A | ASP364 |
A | SER365 |
A | GLU398 |
A | GLN402 |
A | LYS573 |
A | THR594 |
A | HOH777 |
A | HOH825 |
A | HOH860 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 754 |
Chain | Residue |
B | PRO417 |
B | SER418 |
B | SER454 |
B | HOH860 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 757 |
Chain | Residue |
A | SER420 |
A | THR421 |
A | HIS635 |
B | GLN475 |
B | VAL477 |
B | GLN478 |
Functional Information from PROSITE/UniProt
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LvYnDLKpeNIML |
Chain | Residue | Details |
A | LEU272-LEU284 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
Chain | Residue | Details |
A | ASP276 | |
B | ASP276 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | ILE157 | |
A | LYS181 | |
B | ILE157 | |
B | LYS181 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | GLU280 | |
A | ASP276 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | GLU280 | |
B | ASP276 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | LYS278 | |
A | ASP276 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | LYS278 | |
B | ASP276 |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | THR309 | |
A | LYS278 | |
A | ASP276 |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | THR309 | |
B | LYS278 | |
B | ASP276 |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | LYS278 | |
A | ASN281 | |
A | ASP276 |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | LYS278 | |
B | ASN281 | |
B | ASP276 |