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2CN5

Crystal structure of human Chk2 in complex with ADP

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 Residues3
DetailsBINDING SITE FOR RESIDUE CL A1505
ChainResidue
AVAL211
ATYR212
AARG406

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A1506
ChainResidue
AASN352
AASP368
AADP1509
AHOH2078
AHOH2079

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A1507
ChainResidue
AHOH2094
AGLU273

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A1508
ChainResidue
ALEU375
AGLY403
ATYR404
AASN405
AARG406
AHOH2151

site_idAC5
Number of Residues25
DetailsBINDING SITE FOR RESIDUE ADP A1509
ChainResidue
AGLY227
ASER228
AGLY229
AALA230
ACYS231
AGLY232
AVAL234
AALA247
ALYS249
AGLU302
AMET304
AGLU308
AGLU351
AASN352
ALEU354
AASP368
AMG1506
AHOH2019
AHOH2078
AHOH2079
AHOH2092
AHOH2093
AHOH2152
AHOH2153
AHOH2154

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

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

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP347
ALYS349

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP347
ALYS349
ATHR387

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP347
AASN352
ALYS349

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PDB entries from 2024-07-17

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