6I2P
Crystal structure of the Mycobacterium tuberculosis PknB kinase domain (L33E mutant) in complex with its substrate GarA
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 |
D | 0003729 | molecular_function | mRNA binding |
D | 0005515 | molecular_function | protein binding |
D | 0005576 | cellular_component | extracellular region |
D | 0005886 | cellular_component | plasma membrane |
D | 0009274 | cellular_component | peptidoglycan-based cell wall |
D | 0042802 | molecular_function | identical protein binding |
D | 0043457 | biological_process | regulation of cellular respiration |
D | 0045820 | biological_process | negative regulation of glycolytic process |
D | 0140678 | molecular_function | molecular function inhibitor activity |
E | 0003729 | molecular_function | mRNA binding |
E | 0005515 | molecular_function | protein binding |
E | 0005576 | cellular_component | extracellular region |
E | 0005886 | cellular_component | plasma membrane |
E | 0009274 | cellular_component | peptidoglycan-based cell wall |
E | 0042802 | molecular_function | identical protein binding |
E | 0043457 | biological_process | regulation of cellular respiration |
E | 0045820 | biological_process | negative regulation of glycolytic process |
E | 0140678 | molecular_function | molecular function inhibitor activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | binding site for residue ACP A 301 |
Chain | Residue |
A | PHE19 |
A | VAL95 |
A | THR99 |
A | MET145 |
A | MET155 |
A | MG302 |
A | HOH410 |
A | HOH419 |
A | HOH430 |
A | HOH454 |
A | GLY20 |
A | GLY21 |
A | SER23 |
A | VAL25 |
A | ALA38 |
A | LYS40 |
A | VAL72 |
A | GLU93 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue MG A 302 |
Chain | Residue |
A | GLU59 |
A | ASP156 |
A | ACP301 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 303 |
Chain | Residue |
A | ARG29 |
A | ASP30 |
A | LEU31 |
A | HIS34 |
site_id | AC4 |
Number of Residues | 19 |
Details | binding site for residue ACP B 301 |
Chain | Residue |
B | GLY18 |
B | PHE19 |
B | GLY20 |
B | GLY21 |
B | SER23 |
B | VAL25 |
B | ALA38 |
B | LYS40 |
B | VAL72 |
B | MET92 |
B | GLU93 |
B | VAL95 |
B | THR99 |
B | MET145 |
B | MG302 |
B | HOH405 |
B | HOH408 |
B | HOH437 |
B | HOH442 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue MG B 302 |
Chain | Residue |
B | ASP156 |
B | ACP301 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue SO4 D 201 |
Chain | Residue |
D | SER68 |
D | ARG69 |
D | HOH319 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue SO4 D 202 |
Chain | Residue |
A | ARG137 |
D | ASP91 |
D | VAL92 |
D | LYS141 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGFGGMSEVHlArdlrehrd..........VAVK |
Chain | Residue | Details |
A | LEU17-LYS40 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDVKpaNIMI |
Chain | Residue | Details |
A | ILE134-ILE146 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609 |
Chain | Residue | Details |
D | THR2 | |
E | THR2 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by PknG => ECO:0000269|PubMed:19019160 |
Chain | Residue | Details |
D | THR21 | |
E | THR21 | |
A | GLU93 | |
A | LYS140 | |
B | LEU17 | |
B | LYS40 | |
B | GLU93 | |
B | LYS140 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by PknB => ECO:0000269|PubMed:15978616 |
Chain | Residue | Details |
D | THR22 | |
E | THR22 | |
B | ASN143 | |
B | ASP156 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609 |
Chain | Residue | Details |
A | THR2 | |
B | THR2 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:15967413 |
Chain | Residue | Details |
A | SER166 | |
B | SER166 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:12548283 |
Chain | Residue | Details |
A | SER169 | |
B | SER169 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:12950916, ECO:0000269|PubMed:15967413, ECO:0000269|PubMed:15985609, ECO:0000269|PubMed:19008858 |
Chain | Residue | Details |
A | TPO171 | |
B | TPO171 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:12950916, ECO:0000269|PubMed:15967413, ECO:0000269|PubMed:15985609 |
Chain | Residue | Details |
A | TPO173 | |
B | TPO173 |