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8Q61

Co-crystal structure of human AKT2 with compound 3

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005768cellular_componentendosome
A0005769cellular_componentearly endosome
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005938cellular_componentcell cortex
A0005978biological_processglycogen biosynthetic process
A0006006biological_processglucose metabolic process
A0006417biological_processregulation of translation
A0006468biological_processprotein phosphorylation
A0006915biological_processapoptotic process
A0007165biological_processsignal transduction
A0008286biological_processinsulin receptor signaling pathway
A0010748biological_processnegative regulation of long-chain fatty acid import across plasma membrane
A0010907biological_processpositive regulation of glucose metabolic process
A0030334biological_processregulation of cell migration
A0030335biological_processpositive regulation of cell migration
A0032000biological_processpositive regulation of fatty acid beta-oxidation
A0032287biological_processperipheral nervous system myelin maintenance
A0032587cellular_componentruffle membrane
A0032869biological_processcellular response to insulin stimulus
A0035556biological_processintracellular signal transduction
A0036211biological_processprotein modification process
A0043231cellular_componentintracellular membrane-bounded organelle
A0045444biological_processfat cell differentiation
A0045725biological_processpositive regulation of glycogen biosynthetic process
A0046326biological_processpositive regulation of glucose import
A0046872molecular_functionmetal ion binding
A0051726biological_processregulation of cell cycle
A0060644biological_processmammary gland epithelial cell differentiation
A0071486biological_processcellular response to high light intensity
A0072659biological_processprotein localization to plasma membrane
A0090314biological_processpositive regulation of protein targeting to membrane
A0097473biological_processretinal rod cell apoptotic process
A0106310molecular_functionprotein serine kinase activity
A0140677molecular_functionmolecular function activator activity
A2000147biological_processpositive regulation of cell motility
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues34
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGTFGKVIlVrekatgryyamkilrkevIIAK
ChainResidueDetails
ALEU158-LYS191

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvYrDIKleNLML
ChainResidueDetails
AVAL271-LEU283

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP275

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU158
ALYS181

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12434148
ChainResidueDetails
AASN280
AASP293

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22223895
ChainResidueDetails
AMET1

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER34

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER126

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:12434148, ECO:0000269|PubMed:15890450, ECO:0000269|PubMed:20059950, ECO:0000269|PubMed:9512493
ChainResidueDetails
ATHR309

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ASER447
ASER478

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR451

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15890450, ECO:0000269|PubMed:20059950, ECO:0007744|PubMed:19690332
ChainResidueDetails
ASER474

site_idSWS_FT_FI11
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000250
ChainResidueDetails
ASER128
ASER131

site_idSWS_FT_FI12
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) threonine => ECO:0000250
ChainResidueDetails
ATHR306
ATHR313

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PDB entries from 2024-07-17

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