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6CCY

Crystal structure of Akt1 in complex with a selective inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue EX4 A 501
ChainResidue
ALEU156
ALEU181
ATHR211
AMET227
AGLU228
AALA230
AGLU234
AGLU278
AMET281
APHE438
APHE442
AGLY157
AGLY159
APHE161
AGLY162
ALYS163
AVAL164
AALA177
ALYS179

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues34
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGTFGKVIlVkekatgryyamkilkkevIVAK
ChainResidueDetails
ALEU156-LYS189

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvYrDLKleNLML
ChainResidueDetails
AVAL270-LEU282

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by TNK2","evidences":[{"source":"PubMed","id":"20333297","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PDPK1","evidences":[{"source":"PubMed","id":"10792047","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by IKKE, MTOR, PRKDC and TBK1; alternate","evidences":[{"source":"PubMed","id":"14761976","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15047712","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15262962","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15718470","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16266983","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17013611","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20333297","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20978158","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21464307","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23799035","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8978681","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9736715","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"12149249","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GlcNAc) threonine","evidences":[{"source":"PubMed","id":"22629392","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine; alternate","evidences":[{"source":"UniProtKB","id":"P31750","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22410793","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsSite: {"description":"Cleavage; by caspase-3"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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