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1ZYC

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
C0004672molecular_functionprotein kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0004672molecular_functionprotein kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGAFGQVVkArnaldsryy.........AIKK
ChainResidueDetails
ALEU605-LYS629

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpmNIFI
ChainResidueDetails
AILE831-ILE843

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q9BRS2
ChainResidueDetails
AGLU904
BGLU904
CGLU904
DGLU904

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU605
ALYS628
BLEU605
BLYS628
CLEU605
CLYS628
DLEU605
DLYS628

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358
ChainResidueDetails
AGLY830
BGLY830
CGLY830
DGLY830

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:9528799
ChainResidueDetails
AMET951
ALYS956
BMET951
BLYS956
CMET951
CLYS956
DMET951
DLYS956

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AMET839
AASP835

site_idCSA10
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BTHR887
BLYS837
BASP835

site_idCSA11
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CTHR887
CLYS837
CASP835

site_idCSA12
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DTHR887
DLYS837
DASP835

site_idCSA13
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS837
AASN840
AASP835

site_idCSA14
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS837
BASN840
BASP835

site_idCSA15
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CLYS837
CASN840
CASP835

site_idCSA16
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DLYS837
DASN840
DASP835

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BMET839
BASP835

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CMET839
CASP835

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DMET839
DASP835

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS837
AASP835

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS837
BASP835

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CLYS837
CASP835

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DLYS837
DASP835

site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR887
ALYS837
AASP835

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PDB entries from 2024-07-17

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