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2XM9

Structure of a small molecule inhibitor with the kinase domain of Chk2

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 Residues17
DetailsBINDING SITE FOR RESIDUE LWH A 1513
ChainResidue
ALEU226
AGLY307
AGLU308
AGLU351
AASN352
ALEU354
ATHR367
AASP368
AHOH2153
ASER228
ALYS249
AGLU273
AILE286
ALEU301
AGLU302
ALEU303
AMET304

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO3 A 1514
ChainResidue
ALEU375
AGLY403
ATYR404
AASN405
AARG406

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
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP347

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AGLY227
ALYS249
AGLU302
AGLU351
AASP368

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:18644861
ChainResidueDetails
ASER379

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:11390408
ChainResidueDetails
ATHR383
ATHR387

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:17715138
ChainResidueDetails
ASER456

222415

PDB entries from 2024-07-10

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