4MVF
Crystal Structure of Plasmodium falciparum CDPK2 complexed with inhibitor staurosporine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0009931 | molecular_function | calcium-dependent protein serine/threonine kinase activity |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE STU A 601 |
| Chain | Residue |
| A | GLY79 |
| A | SER150 |
| A | GLY151 |
| A | GLU196 |
| A | LEU199 |
| A | ILE212 |
| A | ASP213 |
| A | HOH796 |
| A | GLN80 |
| A | GLY81 |
| A | VAL86 |
| A | ALA99 |
| A | LYS101 |
| A | GLU147 |
| A | LEU148 |
| A | CYS149 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 602 |
| Chain | Residue |
| A | ASP383 |
| A | ASP385 |
| A | SER387 |
| A | THR389 |
| A | GLU394 |
| A | HOH899 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 603 |
| Chain | Residue |
| A | ASP455 |
| A | ASP457 |
| A | ASN459 |
| A | LYS461 |
| A | GLU466 |
| A | HOH776 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 604 |
| Chain | Residue |
| A | ASP493 |
| A | ASN495 |
| A | ASP497 |
| A | GLU499 |
| A | GLU504 |
| A | HOH736 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 605 |
| Chain | Residue |
| A | ASN219 |
| A | LEU220 |
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DVDNSGTLSsqEI |
| Chain | Residue | Details |
| A | ASP383-ILE395 | |
| A | ASP455-LEU467 | |
| A | ASP493-PHE505 |
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGTYGCVYkGidkvtnql..........YAIK |
| Chain | Residue | Details |
| A | LEU78-LYS101 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNFLF |
| Chain | Residue | Details |
| A | ILE188-PHE200 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 35 |
| Details | Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 35 |
| Details | Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 35 |
| Details | Region: {"description":"J domain","evidences":[{"source":"UniProtKB","id":"Q8IBS5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Motif: {"description":"J domain autoinhibitory motif","evidences":[{"source":"UniProtKB","id":"Q8IBS5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 9 |
| Details | Motif: {"description":"J domain EF-hand interaction motif","evidences":[{"source":"UniProtKB","id":"Q8IBS5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"CAD domain of PFF0520w, Calcium dependent protein kinase.","authors":["Wernimont A.K.","Hutchinson A.","Lew J.","Chamberlain K.","MacKenzie F.","Loppnau P.","Cossar D.","Crombet L.","Arrowsmith C.H.","Edwards A.M.","Bountra C.","Weigelt J.","Hui R.","Amani M."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2013","submissionDatabase":"PDB data bank","title":"P. falciparum Calcium-Dependent Protein Kinase 2 (PfCDPK2): First Crystal Structure and Virtual Ligand Screening.","authors":["Lauciello L.","Pernot L.","Bottegoni G.","Bisson W.","Scapozza L.","Perozzo R."]}},{"source":"PDB","id":"3PM8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MVF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2013","submissionDatabase":"PDB data bank","title":"P. falciparum Calcium-Dependent Protein Kinase 2 (PfCDPK2): First Crystal Structure and Virtual Ligand Screening.","authors":["Lauciello L.","Pernot L.","Bottegoni G.","Bisson W.","Scapozza L.","Perozzo R."]}},{"source":"PDB","id":"4MVF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
