3F61
Crystal Structure of M. tuberculosis PknB Leu33Asp/Val222Asp double mutant in complex with ADP
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ADP A 340 |
| Chain | Residue |
| A | GLY18 |
| A | LYS140 |
| A | ALA142 |
| A | ASN143 |
| A | MET145 |
| A | MET155 |
| A | ASP156 |
| A | MG310 |
| A | MG312 |
| A | HOH315 |
| A | HOH358 |
| A | PHE19 |
| A | HOH386 |
| A | HOH394 |
| A | HOH404 |
| A | HOH409 |
| A | HOH410 |
| A | HOH411 |
| A | HOH453 |
| A | SER23 |
| A | VAL25 |
| A | LYS40 |
| A | MET92 |
| A | GLU93 |
| A | VAL95 |
| A | THR99 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 310 |
| Chain | Residue |
| A | ASN143 |
| A | ASP156 |
| A | ADP340 |
| A | HOH410 |
| A | HOH411 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 311 |
| Chain | Residue |
| A | PRO141 |
| A | ALA142 |
| A | HOH385 |
| A | HOH404 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 312 |
| Chain | Residue |
| A | GLY20 |
| A | GLY21 |
| A | MET22 |
| A | SER23 |
| A | ADP340 |
| A | HOH394 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 313 |
| Chain | Residue |
| A | ASN127 |
| A | ALA267 |
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. IiHrDVKpaNIMI |
| Chain | Residue | Details |
| A | ILE134-ILE146 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| 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 | 2 |
| 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 |
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 |
| A | ASP138 | |
| A | LYS140 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP138 | |
| A | ASN143 | |
| A | LYS140 |
