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2XBJ

Crystal Structure of Chk2 in complex with an inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE XBJ A 1513
ChainResidue
ALEU226
AASN352
ALEU354
AMG1514
ANO31516
AHOH2034
AHOH2153
AGLY227
AILE286
ALEU301
AGLU302
AMET304
AGLU305
AGLU308
AGLU351

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1514
ChainResidue
AGLU273
AASP368
AXBJ1513
ANO31516
AHOH2019

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NO3 A 1515
ChainResidue
AGLY403
ATYR404
AASN405
AARG406

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 A 1516
ChainResidue
AVAL234
ALYS249
ATHR367
AASP368
AXBJ1513
AMG1514
AHOH2153

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 Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"18644861","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"11390408","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17715138","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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