1MRV

crystal structure of an inactive Akt2 kinase domain

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	34
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGTFGKVIlVrekatgryyamkilrkevIIAK

Chain	Residue	Details
A	LEU158-LYS191

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site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvYrDIKleNLML

Chain	Residue	Details
A	VAL271-LEU283

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP275

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU158
A	LYS181

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:12434148

Chain	Residue	Details
A	ASN280
A	ASP293

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:12434148, ECO:0000269|PubMed:15890450, ECO:0000269|PubMed:20059950, ECO:0000269|PubMed:9512493

Chain	Residue	Details
A	THR309

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site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332

Chain	Residue	Details
A	SER447
A	SER478

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	THR451

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:15890450, ECO:0000269|PubMed:20059950, ECO:0007744|PubMed:19690332

Chain	Residue	Details
A	SER474

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site_id	SWS_FT_FI8
Number of Residues	2
Details	CARBOHYD: O-linked (GlcNAc) threonine => ECO:0000250

Chain	Residue	Details
A	THR306
A	THR313

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	GLU279
A	ASP275

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	LYS277
A	ASP275

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site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASN280
A	LYS277
A	ASP275

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