2JC6

Crystal structure of human calmodulin-dependent protein kinase 1D

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE QPP A1314

Chain	Residue
A	LEU29
A	GLN99
A	LEU100
A	VAL101
A	TRP306
A	ALA309
A	HOH2009

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE QPP C1314

Chain	Residue
C	LEU100
C	VAL101
C	TRP306
C	ALA309
C	HOH2010
C	LEU29
C	GLN99

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	29
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGAFSEVVlAeekatgklfavkc.....IPKK

Chain	Residue	Details
A	LEU29-LYS57

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

Chain	Residue	Details
A	ILE140-TYR152

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP144
C	ASP144

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
C	LEU29
C	LYS52
A	LEU29
A	LYS52

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648

Chain	Residue	Details
A	SER122
C	SER122

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by CaMKK1 and CaMKK2 => ECO:0000269|PubMed:12935886, ECO:0007744|PubMed:18669648

Chain	Residue	Details
A	THR180
C	THR180

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site_id	SWS_FT_FI5
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447

Chain	Residue	Details
C	LYS113
A	LYS113

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