3BQR

Crystal structure of human death associated protein kinase 3 (DAPK3) in complex with an imidazo-pyridazine ligand

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 4RB A 401

Chain	Residue
A	GLY20
A	HOH588
A	HOH632
A	HOH637
A	HOH656
A	ALA40
A	LYS42
A	GLU94
A	LEU95
A	GLU100
A	MET146
A	ILE160
A	ASP161

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site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PGO A 501

Chain	Residue
A	ARG69
A	ASP81

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site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PGO A 502

Chain	Residue
A	TYR234
A	PHE236
A	ARG253

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site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 503

Chain	Residue
A	LYS42
A	ILE44
A	GLU64
A	ASP161
A	HOH689
A	HOH779

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	28
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGQFAIVRkCrqkgtgkeyaak......FIKK

Chain	Residue	Details
A	LEU19-LYS46

---

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

Chain	Residue	Details
A	ILE135-LEU147

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP139

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU19

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	LYS42

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:18239682, ECO:0007744|PDB:2J90

Chain	Residue	Details
A	GLU94
A	VAL96

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:18239682

Chain	Residue	Details
A	SER50

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:15611134, ECO:0000269|PubMed:17158456

Chain	Residue	Details
A	THR180

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:15611134

Chain	Residue	Details
A	THR225

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by autocatalysis and ROCK1 => ECO:0000269|PubMed:15611134, ECO:0000269|PubMed:17158456, ECO:0000269|PubMed:18239682

Chain	Residue	Details
A	THR265

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	GLU143
A	ASP139

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP139
A	LYS141

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	THR180
A	ASP139
A	LYS141

---

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP139
A	LYS141
A	ASN144

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