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6NPZ

Crystal structure of Akt1 (aa 123-480) kinase with a bisubstrate

Replaces:  6C0I
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 Residues5
Detailsbinding site for residue MN A 501
ChainResidue
AGLU314
AHIS354
AHOH706
AHOH749
BHOH630

site_idAC2
Number of Residues2
Detailsbinding site for residue PGE A 502
ChainResidue
AGLN414
ATYR417

site_idAC3
Number of Residues7
Detailsbinding site for residue PGE A 503
ChainResidue
ATYR350
ALEU360
AHOH639
AHOH721
FARG2
ALEU347
APHE349

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL B 501
ChainResidue
BLYS385
BLYS386
BASP387
BGLN390
BHOH661
BHOH719

site_idAC5
Number of Residues4
Detailsbinding site for residue VO4 B 502
ChainResidue
AASN351
AGLN352
BHOH608
BHOH739

site_idAC6
Number of Residues6
Detailsbinding site for residue MN B 503
ChainResidue
BGLU314
BHIS354
BHOH665
BHOH709
BHOH722
BHOH731

site_idAC7
Number of Residues4
Detailsbinding site for residue MN F 101
ChainResidue
AASP292
AHOH631
FZXW7
FHOH202

site_idAC8
Number of Residues4
Detailsbinding site for residue MN G 501
ChainResidue
BASN279
BASP292
GZXW7
GHOH606

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 Residues2
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 Residues18
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Cleavage; by caspase-3","evidences":[{"source":"UniProtKB","id":"P31750","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by TNK2","evidences":[{"source":"PubMed","id":"20333297","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by IKKE, PDPK1 and TBK1","evidences":[{"source":"PubMed","id":"15718470","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18456494","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20333297","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20481595","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21464307","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8978681","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9512493","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsGlycosylation: {"description":"O-linked (GlcNAc) threonine","evidences":[{"source":"PubMed","id":"22629392","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22410793","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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