3F69
Crystal structure of the Mycobacterium tuberculosis PknB mutant kinase domain in complex with KT5720
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE XDR A 309 |
| Chain | Residue |
| A | LEU17 |
| A | VAL155 |
| A | GLY18 |
| A | VAL25 |
| A | ALA38 |
| A | GLU93 |
| A | VAL95 |
| A | GLY97 |
| A | ALA142 |
| A | ASN143 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 310 |
| Chain | Residue |
| A | ARG10 |
| A | ARG32 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 311 |
| Chain | Residue |
| A | ALA256 |
| A | LYS257 |
| A | ASN258 |
| A | ASN261 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE XDR B 309 |
| Chain | Residue |
| B | LEU17 |
| B | GLY18 |
| B | ALA38 |
| B | LYS40 |
| B | GLU93 |
| B | VAL95 |
| B | THR99 |
| B | ALA142 |
| B | ASN143 |
| B | LEU145 |
| B | VAL155 |
| B | ASP156 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 B 310 |
| Chain | Residue |
| B | ARG32 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 311 |
| Chain | Residue |
| B | ALA256 |
| B | LYS257 |
| B | ASN258 |
| B | ASN261 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGFGGMSEVHlArdlrdhrd..........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. IiHrDVKpaNILI |
| 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 | 1 |
| 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 | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"12548283","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15967413","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"12548283","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| 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_FI8 |
| Number of Residues | 1 |
| 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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ALA142 | |
| A | ASP138 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ALA142 | |
| B | ASP138 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP138 | |
| A | LYS140 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP138 | |
| B | LYS140 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | THR179 | |
| A | ASP138 | |
| A | LYS140 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | THR179 | |
| B | ASP138 | |
| B | LYS140 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP138 | |
| A | ASN143 | |
| A | LYS140 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP138 | |
| B | ASN143 | |
| B | LYS140 |
