Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4A9U

CRYSTAL STRUCTURE OF HUMAN CHK2 IN COMPLEX WITH BENZIMIDAZOLE CARBOXAMIDE 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 Residues5
DetailsBINDING SITE FOR RESIDUE NO3 A 1514
ChainResidue
ALEU375
AGLY403
ATYR404
AASN405
AARG406

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1515
ChainResidue
AILE288
AHOH2015
ALEU277
ALYS278
ALEU280
ALYS287

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE A9U A 1516
ChainResidue
ALYS249
ALEU301
AMET304
AGLU305
AGLY307
AGLU308
ALEU354
AGLN358
ATHR367
AASP368
AHOH2025

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 1517
ChainResidue
ALYS278
AILE288
AASN290

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1518
ChainResidue
ALYS465
APHE475
AGLU479
AARG482
AHIS483
APRO484
AHOH2082

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1519
ChainResidue
AGLU219
AASN290
APHE291
APHE292

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 1520
ChainResidue
AARG346
AVAL408
AHOH2085

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1521
ChainResidue
ALYS214
AGLU479
AARG482
AHOH2003
AHOH2079

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 1522
ChainResidue
AGLN336
AARG482

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1523
ChainResidue
AARG240
ALYS241
AGLY400
ALYS472
AHOH2071
AHOH2086
AHOH2087

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1524
ChainResidue
ATHR242
ALYS244
AGLU429
ASER435
ALEU436
ALYS437

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1525
ChainResidue
AVAL211
ATYR212
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

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon