1FQ1
CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) IN COMPLEX WITH PHOSPHO-CDK2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000079 | biological_process | regulation of cyclin-dependent protein serine/threonine kinase activity |
| A | 0000082 | biological_process | G1/S transition of mitotic cell cycle |
| A | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| A | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
| A | 0004725 | molecular_function | protein tyrosine phosphatase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006470 | biological_process | protein dephosphorylation |
| A | 0008138 | molecular_function | protein tyrosine/serine/threonine phosphatase activity |
| A | 0008285 | biological_process | negative regulation of cell population proliferation |
| A | 0016311 | biological_process | dephosphorylation |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0048471 | cellular_component | perinuclear region of cytoplasm |
| A | 0051726 | biological_process | regulation of cell cycle |
| B | 0000082 | biological_process | G1/S transition of mitotic cell cycle |
| B | 0000086 | biological_process | G2/M transition of mitotic cell cycle |
| B | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0000307 | cellular_component | cyclin-dependent protein kinase holoenzyme complex |
| B | 0000723 | biological_process | telomere maintenance |
| B | 0000781 | cellular_component | chromosome, telomeric region |
| B | 0000793 | cellular_component | condensed chromosome |
| B | 0000805 | cellular_component | X chromosome |
| B | 0000806 | cellular_component | Y chromosome |
| B | 0001673 | cellular_component | male germ cell nucleus |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0004693 | molecular_function | cyclin-dependent protein serine/threonine kinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005635 | cellular_component | nuclear envelope |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005667 | cellular_component | transcription regulator complex |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005768 | cellular_component | endosome |
| B | 0005813 | cellular_component | centrosome |
| B | 0005829 | cellular_component | cytosol |
| B | 0005856 | cellular_component | cytoskeleton |
| B | 0006260 | biological_process | DNA replication |
| B | 0006281 | biological_process | DNA repair |
| B | 0006338 | biological_process | chromatin remodeling |
| B | 0006351 | biological_process | DNA-templated transcription |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0006813 | biological_process | potassium ion transport |
| B | 0006974 | biological_process | DNA damage response |
| B | 0007099 | biological_process | centriole replication |
| B | 0007165 | biological_process | signal transduction |
| B | 0007265 | biological_process | Ras protein signal transduction |
| B | 0007346 | biological_process | regulation of mitotic cell cycle |
| B | 0008284 | biological_process | positive regulation of cell population proliferation |
| B | 0010389 | biological_process | regulation of G2/M transition of mitotic cell cycle |
| B | 0010468 | biological_process | regulation of gene expression |
| B | 0015030 | cellular_component | Cajal body |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0018105 | biological_process | peptidyl-serine phosphorylation |
| B | 0019904 | molecular_function | protein domain specific binding |
| B | 0030332 | molecular_function | cyclin binding |
| B | 0031453 | biological_process | positive regulation of heterochromatin formation |
| B | 0031571 | biological_process | mitotic G1 DNA damage checkpoint signaling |
| B | 0031848 | biological_process | protection from non-homologous end joining at telomere |
| B | 0032298 | biological_process | positive regulation of DNA-templated DNA replication initiation |
| B | 0035173 | molecular_function | histone kinase activity |
| B | 0043247 | biological_process | telomere maintenance in response to DNA damage |
| B | 0043687 | biological_process | post-translational protein modification |
| B | 0045740 | biological_process | positive regulation of DNA replication |
| B | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051298 | biological_process | centrosome duplication |
| B | 0051301 | biological_process | cell division |
| B | 0051321 | biological_process | meiotic cell cycle |
| B | 0071732 | biological_process | cellular response to nitric oxide |
| B | 0090398 | biological_process | cellular senescence |
| B | 0097123 | cellular_component | cyclin A1-CDK2 complex |
| B | 0097124 | cellular_component | cyclin A2-CDK2 complex |
| B | 0097134 | cellular_component | cyclin E1-CDK2 complex |
| B | 0097135 | cellular_component | cyclin E2-CDK2 complex |
| B | 0097472 | molecular_function | cyclin-dependent protein kinase activity |
| B | 0106310 | molecular_function | protein serine kinase activity |
| B | 1905784 | biological_process | regulation of anaphase-promoting complex-dependent catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 383 |
| Chain | Residue |
| B | ASN132 |
| B | ASP145 |
| B | ATP381 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ATP B 381 |
| Chain | Residue |
| B | GLU81 |
| B | PHE82 |
| B | LEU83 |
| B | ASP86 |
| B | LYS89 |
| B | ASP127 |
| B | LYS129 |
| B | GLN131 |
| B | ASN132 |
| B | ASP145 |
| B | MG383 |
| B | ILE10 |
| B | GLY13 |
| B | THR14 |
| B | VAL18 |
| B | ALA31 |
| B | LYS33 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK |
| Chain | Residue | Details |
| B | ILE10-LYS33 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI |
| Chain | Residue | Details |
| B | VAL123-ILE135 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 168 |
| Details | Domain: {"description":"Tyrosine-protein phosphatase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00160","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Phosphocysteine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00160","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17095507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21565702","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21565702","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Site: {"description":"CDK7 binding","evidences":[{"source":"PubMed","id":"17373709","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"1396589","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17095507","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by WEE1","evidences":[{"source":"PubMed","id":"1396589","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17095507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by CAK and CCRK","evidences":[{"source":"PubMed","id":"1396589","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14597612","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16325401","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17095507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17570665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20147522","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20360007","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21565702","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28666995","evidenceCode":"ECO:0000305"}]} |
| 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 |
| B | GLN131 | |
| B | ASP127 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP127 | |
| B | LYS129 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP127 | |
| B | LYS129 | |
| B | THR165 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP127 | |
| B | LYS129 | |
| B | ASN132 |
