The genus trace: a function that shows values of genus (vertical axis) for subchains spanned between the first residue, and all other residues (shown on horizontal axis). The number of the latter residue and the genus of a given subchain are shown interactively.
Total Genus |
277
|
sequence length |
1081
|
structure length |
1042
|
Chain Sequence |
MSYYHHHHHHDYDIPTTRPSSGELWGIHLMPPRILVECLLPNGMIVTLECLREATLITIKHELFKEARKYPLHQLLQDESSYIFVSVTQEAEREEFFDETRRLCDLRLFQPFLKVIEPVGNREEKILNREIGFAIGMPVCEFDMVKDPEVQDFRRNILNVCKEAVDLRDLNSPHSRAMYVYPPNVESSPELPKHIYNKLDKGQIIVVIWVIVSPNNDKQKYTLKINHDCVPEQVIAEAIRKKTRSMLLSSEQLKLCVLEYQGKYILKVCGCDEYFLEKYPLSQYKYIRSCIMLGRMPNLMLMAKESLYSQLPMDCFTMPSYSETSTKSLWVINSALRIKILCATYVNVNIRDIDKIYVRTGIYHGGEPLCDNVNTQRVPCSNPRWNEWLNYDIYIPDLPRAARLCLSICSVEHCPLAWGNINLFDYTDTLVSGKMALNLWPVPHGLEDLLNPIGVTGSNPNKETPCLELEFDWFSSVVKFPDMSVIEEHANWSVSREAGFSYSHAGLSDNELRENDKEQLKAISTRDPLSEITEQEKDFLWSHRHYCVTIPEILPKLLLSVKWNSRDEVAQMYCLVKDWPPIKPEQAMELLDCNYPDPMVRGFAVRCLEKYLTDDKLSQYLIQLVQVLKYEQYLDNLLVRFLLKKALTNQRIGHFFFWHLKSEMHNKTVSQRFGLLLESYCRACGMYLKHLNRQVEAMEKLINLTDILKQEKKDETQKVQMKFLVEQMRRPDFMDALQGFLSPLNPAHQLGNLRLEECRIMSSAKRPLWLNWENPDIMSELLFQNNEIIFKNGDDLRQDMLTLQIIRIMENIWQNQGLDLRMLPYGCLSIGDCVGLIEVVRNSHTIMQIQCKGGLKGALQFNSHTLHQWLKDKNKGEIYDAAIDLFTRSCAGYCVATFILGIGDRHNSNIMVKDDGQLFHIDFGHFLDHKKKKFGYKRERVPFVLTQDFLIVISKGAQECTKTREFERFQEMCYKAYLAIRQHANLFINLFSMMLGSGMPELQSFDDIAYIRKTLALDKTEQEALEYFMKQMNDAHHGGWTT
|
The genus matrix. At position (x,y) a genus value for a subchain spanned between x’th and y’th residue is shown. Values of the genus are represented by color, according to the scale given on the right.
After clicking on a point (x,y) in the genus matrix above, a subchain from x to y is shown in color.
publication title |
Structural basis of nSH2 regulation and lipid binding in PI3K alpha.
pubmed rcsb |
molecule tags |
Transferase/transferase regulator
|
source organism |
Homo sapiens
|
molecule keywords |
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic sub
|
total genus |
277
|
structure length |
1042
|
sequence length |
1081
|
ec nomenclature |
ec
2.7.1.153: Phosphatidylinositol-4,5-bisphosphate 3-kinase. |
pdb deposition date | 2014-01-14 |
chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
---|---|---|---|
A | PF00454 | PI3_PI4_kinase | Phosphatidylinositol 3- and 4-kinase |
A | PF00613 | PI3Ka | Phosphoinositide 3-kinase family, accessory domain (PIK domain) |
A | PF00792 | PI3K_C2 | Phosphoinositide 3-kinase C2 |
A | PF00794 | PI3K_rbd | PI3-kinase family, ras-binding domain |
A | PF02192 | PI3K_p85B | PI3-kinase family, p85-binding domain |
cath code
| Class | Architecture | Topology | Homology | Domain |
---|---|---|---|---|---|
Mainly Alpha | Orthogonal Bundle | Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, Domain 5 | Phosphatidylinositol 3-/4-kinase, catalytic domain | ||
Mainly Alpha | Alpha Horseshoe | Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat | Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat | ||
Mainly Beta | Sandwich | Immunoglobulin-like | C2 domain | ||
Alpha Beta | Roll | Ubiquitin-like (UB roll) | Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 | ||
Alpha Beta | Roll | Ubiquitin-like (UB roll) | Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 | ||
Alpha Beta | 2-Layer Sandwich | Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 4 | Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 4 |