4FT5

Crystal Structure of the CHK1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000077	biological_process	DNA damage checkpoint signaling
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE H2K A 300

Chain	Residue
A	LEU15
A	GLU91
A	LEU137
A	ASP148
A	HOH474
A	ALA36
A	LYS38
A	VAL68
A	GLU85
A	TYR86
A	CYS87
A	SER88
A	GLY90

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 301

Chain	Residue
A	LYS54
A	ARG129
A	THR153
A	HOH433
A	HOH461

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site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 302

Chain	Residue
A	TRP221
A	LYS224
A	HIS243

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAYGEVQlAvnrvteea..........VAVK

Chain	Residue	Details
A	LEU15-LYS38

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site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ItHrDIKpeNLLL

Chain	Residue	Details
A	ILE126-LEU138

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	ASP130

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU15
A	LYS38

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER280

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site_id	SWS_FT_FI4
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:32357935

Chain	Residue	Details
A	LYS132

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