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3E8D

Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE G98 A 1
ChainResidue
ALYS160
APHE227
AMET229
AGLU230
ATYR231
AALA232
AASN280
AMET282
ATHR292
AASP293
APHE294
AGLY161
APHE439
CSER9
AGLY164
ALYS165
AVAL166
AALA179
ALYS181
AGLU200
ALEU204

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE G98 B 1
ChainResidue
BGLY161
BGLY164
BVAL166
BALA179
BLYS181
BGLU200
BLEU204
BPHE227
BMET229
BGLU230
BTYR231
BALA232
BASN280
BMET282
BTHR292
BASP293
BPHE294
BPHE439
DSER9

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 Residues2
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
CSER9
DSER9

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU158
ALYS181
BLEU158
BLYS181

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12434148
ChainResidueDetails
AASN280
AASP293
BASN280
BASP293

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:12434148, ECO:0000269|PubMed:15890450, ECO:0000269|PubMed:20059950, ECO:0000269|PubMed:9512493
ChainResidueDetails
ATPO309
BTPO309

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ASER447
ASER478
BSER447
BSER478

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569
ChainResidueDetails
ATPO451
BTPO451

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15890450, ECO:0000269|PubMed:20059950, ECO:0007744|PubMed:19690332
ChainResidueDetails
AASP474
BASP474

site_idSWS_FT_FI8
Number of Residues4
DetailsCARBOHYD: O-linked (GlcNAc) threonine => ECO:0000250
ChainResidueDetails
ATHR306
ATHR313
BTHR306
BTHR313

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PDB entries from 2024-03-27

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