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 | 0046777 | biological_process | protein autophosphorylation |
| 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 | 0046777 | biological_process | protein autophosphorylation |
| 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 |
