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 | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12548283","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12551895","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylthreonine","evidences":[{"source":"PubMed","id":"21969609","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"12548283","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"12548283","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12950916","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15967413","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15985609","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19008858","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"12548283","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12950916","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15967413","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15985609","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 98 |
| Details | Domain: {"description":"FHA","evidences":[{"source":"PROSITE-ProRule","id":"PRU00086","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
