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3CQW

Crystal Structure of Akt-1 complexed with substrate peptide and 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 Residues2
DetailsBINDING SITE FOR RESIDUE MN A 1
ChainResidue
AGLU314
AHIS354

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CQW A 999
ChainResidue
AASN279
AMET281
ATHR291
AASP292
AALA177
ATHR211
AMET227
AGLU228
AALA230
AGLU234
AGLU278

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
DetailsMOD_RES: Phosphoserine; by PKB/AKT1, RPS6KA3 and SGK3 => ECO:0000269|PubMed:12054501, ECO:0000269|PubMed:16484495, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:24391509, ECO:0000269|PubMed:25169422, ECO:0000269|PubMed:8250835
ChainResidueDetails
CSER7

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU156
ALYS179

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Cleavage; by caspase-3 => ECO:0000250|UniProtKB:P31750
ChainResidueDetails
AASP462

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by TNK2 => ECO:0000269|PubMed:20333297
ChainResidueDetails
ATYR176

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by IKKE, PDPK1 and TBK1 => ECO:0000269|PubMed:15718470, ECO:0000269|PubMed:18456494, ECO:0000269|PubMed:20333297, ECO:0000269|PubMed:20481595, ECO:0000269|PubMed:21464307, ECO:0000269|PubMed:8978681, ECO:0000269|PubMed:9512493
ChainResidueDetails
ATPO308

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR448
ATHR450

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine; by IKKE, MTOR and TBK1; alternate => ECO:0000269|PubMed:14761976, ECO:0000269|PubMed:15047712, ECO:0000269|PubMed:15718470, ECO:0000269|PubMed:16266983, ECO:0000269|PubMed:17013611, ECO:0000269|PubMed:20333297, ECO:0000269|PubMed:20978158, ECO:0000269|PubMed:21464307, ECO:0000269|PubMed:23799035, ECO:0000269|PubMed:8978681, ECO:0000269|PubMed:9736715
ChainResidueDetails
AASP473

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:12149249
ChainResidueDetails
ATYR474

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) threonine => ECO:0000269|PubMed:22629392
ChainResidueDetails
ATHR305
ATHR312

site_idSWS_FT_FI10
Number of Residues1
DetailsCARBOHYD: O-linked (GlcNAc) serine; alternate => ECO:0000250|UniProtKB:P31750
ChainResidueDetails
AASP473

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:22410793
ChainResidueDetails
ALYS284

218853

PDB entries from 2024-04-24

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