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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7OAJ

Crystal structure of pseudokinase CASK in complex with compound 7

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
B	0004672	molecular_function	protein kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue V6E A 401

Chain	Residue
A	ILE18
A	CYS146
A	LEU148
A	GLY161
A	GLY162
A	HOH517
A	GLY19
A	ALA39
A	GLU92
A	PHE93
A	MET94
A	ASP95
A	GLY96
A	LYS105

site_id	AC2
Number of Residues	3
Details	binding site for residue EDO A 402

Chain	Residue
A	ARG28
A	ILE30
B	HIS287

site_id	AC3
Number of Residues	6
Details	binding site for residue EDO A 403

Chain	Residue
A	SER24
A	LYS41
A	PHE48
A	LEU59
A	GLU62
A	HOH605

site_id	AC4
Number of Residues	6
Details	binding site for residue EDO A 404

Chain	Residue
A	CYS66
A	ILE74
A	VAL75
A	LEU77
A	PHE163
A	HOH563

site_id	AC5
Number of Residues	5
Details	binding site for residue EDO A 405

Chain	Residue
A	ARG130
A	ASP134
A	TYR268
A	HOH511
A	HOH575

site_id	AC6
Number of Residues	6
Details	binding site for residue EDO A 406

Chain	Residue
A	ASN136
A	GLU171
A	GLY173
B	GLU247
B	ASP251
B	HOH558

site_id	AC7
Number of Residues	3
Details	binding site for residue EDO A 407

Chain	Residue
A	LEU217
A	TYR220
A	HOH576

site_id	AC8
Number of Residues	15
Details	binding site for residue V6E B 401

Chain	Residue
B	ILE18
B	GLY19
B	ALA39
B	PHE91
B	GLU92
B	PHE93
B	MET94
B	ASP95
B	GLY96
B	LYS105
B	CYS146
B	LEU148
B	GLY161
B	GLY162
B	HOH590

site_id	AC9
Number of Residues	5
Details	binding site for residue EDO B 402

Chain	Residue
A	GLU247
A	ASP251
B	ASN136
B	GLU171
B	LYS198

site_id	AD1
Number of Residues	4
Details	binding site for residue EDO B 403

Chain	Residue
A	VAL112
A	HIS287
B	ARG28
B	ILE30

site_id	AD2
Number of Residues	5
Details	binding site for residue EDO B 404

Chain	Residue
B	SER24
B	LYS41
B	VAL43
B	GLU62
B	HOH563

site_id	AD3
Number of Residues	4
Details	binding site for residue EDO B 405

Chain	Residue
B	LYS70
B	HIS71
B	HOH507
B	HOH551

site_id	AD4
Number of Residues	3
Details	binding site for residue EDO B 406

Chain	Residue
B	PHE101
B	HIS145
B	ARG302

site_id	AD5
Number of Residues	2
Details	binding site for residue EDO B 407

Chain	Residue
B	ALA97
B	PHE101

site_id	AD6
Number of Residues	4
Details	binding site for residue EDO B 408

Chain	Residue
B	LYS70
B	CYS216
B	LEU217
B	TYR220

site_id	AD7
Number of Residues	4
Details	binding site for residue EDO B 409

Chain	Residue
A	GLU269
B	TYR235
B	ARG254
B	HOH514

site_id	AD8
Number of Residues	14
Details	binding site for residue V6E C 401

Chain	Residue
C	LEU148
C	GLY161
C	GLY162
C	HOH547
C	ILE18
C	GLY19
C	ALA39
C	GLU92
C	MET94
C	ASP95
C	GLY96
C	ALA97
C	LYS105
C	CYS146

site_id	AD9
Number of Residues	4
Details	binding site for residue EDO C 402

Chain	Residue
C	ARG28
C	ILE30
D	ILE286
D	HIS287

site_id	AE1
Number of Residues	3
Details	binding site for residue EDO C 403

Chain	Residue
C	SER24
C	LYS41
C	GLU62

site_id	AE2
Number of Residues	3
Details	binding site for residue EDO C 404

Chain	Residue
C	HIS120
C	SER155
C	HOH560

site_id	AE3
Number of Residues	4
Details	binding site for residue EDO C 405

Chain	Residue
C	CYS216
C	LEU217
C	TYR220
C	HOH561

site_id	AE4
Number of Residues	3
Details	binding site for residue EDO C 406

Chain	Residue
C	TYR235
C	ARG254
D	GLU269

site_id	AE5
Number of Residues	13
Details	binding site for residue V6E D 401

Chain	Residue
D	ILE18
D	ALA39
D	PHE91
D	GLU92
D	PHE93
D	MET94
D	ASP95
D	GLY96
D	LYS105
D	CYS146
D	LEU148
D	GLY161
D	GLY162

site_id	AE6
Number of Residues	4
Details	binding site for residue EDO D 402

Chain	Residue
C	VAL112
C	HIS287
D	ARG28
D	ILE30

site_id	AE7
Number of Residues	6
Details	binding site for residue EDO D 403

Chain	Residue
D	SER24
D	LYS41
D	VAL43
D	PHE48
D	GLU62
D	HOH591

site_id	AE8
Number of Residues	7
Details	binding site for residue EDO D 404

Chain	Residue
C	GLU247
C	HOH545
D	ASN136
D	GLY170
D	GLU171
D	GLY173
D	LYS198

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000250

Chain	Residue	Details
A	ASP141
B	ASP141
C	ASP141
D	ASP141

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00100, ECO:0000255\|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ILE18
B	ILE18
C	ILE18
D	ILE18

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LYS41
B	LYS41
C	LYS41
D	LYS41

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER51
B	SER51
C	SER51
D	SER51

site_id	SWS_FT_FI5
Number of Residues	8
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269\|PubMed:18423203

Chain	Residue	Details
A	SER151
A	SER155
B	SER151
B	SER155
C	SER151
C	SER155
D	SER151
D	SER155

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:O70589

Chain	Residue	Details
A	THR182
B	THR182
C	THR182
D	THR182

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER313
B	SER313
C	SER313
D	SER313

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PDB entries from 2024-08-14

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