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1ZYD

Crystal Structure of eIF2alpha Protein Kinase GCN2: Wild-Type Complexed with ATP.

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
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 305
ChainResidue
AATP303
AASP853

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 306
ChainResidue
AATP303
AASN840
AASP853

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B 307
ChainResidue
BATP304
BASP853

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 308
ChainResidue
BASP853
BATP304
BASN840

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ATP A 303
ChainResidue
AHOH7
AHOH35
AMG305
AMG306
ALEU605
AVAL613
AALA626
AGLU789
ACYS791
AASP835
ALYS837
AASN840
AASP853

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ATP B 304
ChainResidue
BHOH38
BMG307
BMG308
BLEU605
BVAL613
BALA626
BGLU789
BCYS791
BASP835
BLYS837
BASN840
BASP853

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 Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q9BRS2","evidenceCode":"ECO:0000250"}]}
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
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"9528799","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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

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
ALYS837
AASP835

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS837
BASP835

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR887
ALYS837
AASP835

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BTHR887
BLYS837
BASP835

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS837
AASN840
AASP835

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS837
BASN840
BASP835

247536

PDB entries from 2026-01-14

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