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4HYI

X-RAY Crystal structure of compound 40 bound to human chk1 kinase domain

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 Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
AGLN108
ALYS267
ALEU269
ALYS271
AHOH444

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
AHOH647
ATRP221
AHIS243
ALEU246
AHOH447

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 303
ChainResidue
AARG29
AARG181
AASN249
AHOH435

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 1AO A 304
ChainResidue
ALEU15
ATYR20
AALA36
ALYS38
AGLU55
ALEU84
AGLU85
ACYS87
AGLU91
AGLU134
ALEU137
ASER147
AASP148
AHOH650
AHOH652

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
ALEU15
ALYS38

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

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER286

site_idSWS_FT_FI5
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:32357935
ChainResidueDetails
ALYS132

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PDB entries from 2024-07-17

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