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4FTR

Crystal Structure of the CHK1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000077biological_processDNA damage checkpoint signaling
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 5HK A 301
ChainResidue
AGLN13
ATYR20
AVAL23
ALYS38
ATYR86
ACYS87
AGLY90
ALEU137
AASP148

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
ALYS54
AARG129
ATHR153
AARG162
AHOH445

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 303
ChainResidue
ALYS132
AGLU134
ATYR173
AHOH514

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IPA A 304
ChainResidue
AILE96
ATYR173
AGLY204
AGLU205

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAYGEVQlAvnrvteea..........VAVK
ChainResidueDetails
ALEU15-LYS38

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ItHrDIKpeNLLL
ChainResidueDetails
AILE126-LEU138

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP130

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALYS38
ALEU15

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER280

site_idSWS_FT_FI4
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:32357935
ChainResidueDetails
ALYS132

221051

PDB entries from 2024-06-12

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