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3I6W

Structure and Activation Mechanism of the CHK2 DNA-Damage Checkpoint Kinase

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
E0004672molecular_functionprotein kinase activity
E0005524molecular_functionATP binding
E0006468biological_processprotein phosphorylation
F0004672molecular_functionprotein kinase activity
F0005524molecular_functionATP binding
F0006468biological_processprotein phosphorylation
G0004672molecular_functionprotein kinase activity
G0005524molecular_functionATP binding
G0006468biological_processprotein phosphorylation
H0004672molecular_functionprotein kinase activity
H0005524molecular_functionATP binding
H0006468biological_processprotein phosphorylation
Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpeNVLL
ChainResidueDetails
AILE343-LEU355

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP347
BASP347
CASP347
DASP347
EASP347
FASP347
GASP347
HASP347

site_idSWS_FT_FI2
Number of Residues40
DetailsBINDING:
ChainResidueDetails
AGLY227
BASP368
CGLY227
CARG249
CGLU302
CGLU351
CASP368
DGLY227
DARG249
DGLU302
DGLU351
AARG249
DASP368
EGLY227
EARG249
EGLU302
EGLU351
EASP368
FGLY227
FARG249
FGLU302
FGLU351
AGLU302
FASP368
GGLY227
GARG249
GGLU302
GGLU351
GASP368
HGLY227
HARG249
HGLU302
HGLU351
AGLU351
HASP368
AASP368
BGLY227
BARG249
BGLU302
BGLU351

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: Phosphoserine; by PLK3 => ECO:0000269|PubMed:16481012
ChainResidueDetails
ASER73
BSER73
CSER73
DSER73
ESER73
FSER73
GSER73
HSER73

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:18644861
ChainResidueDetails
ASER379
BSER379
CSER379
DSER379
ESER379
FSER379
GSER379
HSER379

site_idSWS_FT_FI5
Number of Residues16
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:11390408
ChainResidueDetails
ATHR383
ETHR387
FTHR383
FTHR387
GTHR383
GTHR387
HTHR383
HTHR387
ATHR387
BTHR383
BTHR387
CTHR383
CTHR387
DTHR383
DTHR387
ETHR383

site_idSWS_FT_FI6
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:17715138
ChainResidueDetails
ASER456
BSER456
CSER456
DSER456
ESER456
FSER456
GSER456
HSER456

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP347
AGLU351

site_idCSA10
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP347
BLYS349

site_idCSA11
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASP347
CLYS349

site_idCSA12
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DASP347
DLYS349

site_idCSA13
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
EASP347
ELYS349

site_idCSA14
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
FASP347
FLYS349

site_idCSA15
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
GASP347
GLYS349

site_idCSA16
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
HASP347
HLYS349

site_idCSA17
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP347
AASN352
ALYS349

site_idCSA18
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP347
BASN352
BLYS349

site_idCSA19
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASP347
CASN352
CLYS349

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP347
BGLU351

site_idCSA20
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DASP347
DASN352
DLYS349

site_idCSA21
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
EASP347
EASN352
ELYS349

site_idCSA22
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
FASP347
FASN352
FLYS349

site_idCSA23
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
GASP347
GASN352
GLYS349

site_idCSA24
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
HASP347
HASN352
HLYS349

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASP347
CGLU351

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DASP347
DGLU351

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
EASP347
EGLU351

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
FASP347
FGLU351

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
GASP347
GGLU351

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
HASP347
HGLU351

site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP347
ALYS349

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PDB entries from 2024-07-10

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