1ZYC

Crystal Structure of eIF2alpha Protein Kinase GCN2: Wild-Type in Apo Form.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	25
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGAFGQVVkArnaldsryy.........AIKK

Chain	Residue	Details
A	LEU605-LYS629

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

Chain	Residue	Details
A	ILE831-ILE843

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q9BRS2

Chain	Residue	Details
A	GLU904
B	GLU904
C	GLU904
D	GLU904

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU605
A	LYS628
B	LEU605
B	LYS628
C	LEU605
C	LYS628
D	LEU605
D	LYS628

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358

Chain	Residue	Details
A	GLY830
B	GLY830
C	GLY830
D	GLY830

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site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:9528799

Chain	Residue	Details
A	MET951
A	LYS956
B	MET951
B	LYS956
C	MET951
C	LYS956
D	MET951
D	LYS956

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