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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7OAI

Crystal structure of pseudokinase CASK in complex with PFE-PKIS12

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	13
Details	binding site for residue V5W A 401

Chain	Residue
A	ILE18
A	LEU148
A	GLY161
A	GLY162
A	HOH593
A	ALA39
A	GLU92
A	MET94
A	ASP95
A	GLY96
A	ALA97
A	LYS105
A	CYS146

site_id	AC2
Number of Residues	4
Details	binding site for residue EDO A 402

Chain	Residue
A	ARG28
A	ILE30
A	EDO403
D	HIS287

site_id	AC3
Number of Residues	3
Details	binding site for residue EDO A 403

Chain	Residue
A	GLU13
A	EDO402
D	LYS285

site_id	AC4
Number of Residues	5
Details	binding site for residue EDO A 404

Chain	Residue
A	SER24
A	LYS41
A	VAL43
A	GLU62
A	HOH564

site_id	AC5
Number of Residues	2
Details	binding site for residue EDO A 405

Chain	Residue
A	HIS287
D	ARG28

site_id	AC6
Number of Residues	5
Details	binding site for residue EDO A 406

Chain	Residue
A	ASP134
A	HOH505
A	HOH518
D	ASP251
D	ARG254

site_id	AC7
Number of Residues	12
Details	binding site for residue V5W B 401

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

site_id	AC8
Number of Residues	5
Details	binding site for residue EDO B 402

Chain	Residue
B	SER24
B	LYS41
B	PHE48
B	GLU62
B	HOH551

site_id	AC9
Number of Residues	3
Details	binding site for residue EDO B 403

Chain	Residue
B	CYS15
B	ARG28
C	HIS287

site_id	AD1
Number of Residues	1
Details	binding site for residue EDO B 404

Chain	Residue
B	ILE18

site_id	AD2
Number of Residues	2
Details	binding site for residue EDO B 405

Chain	Residue
B	GLU171
B	LYS234

site_id	AD3
Number of Residues	4
Details	binding site for residue EDO B 406

Chain	Residue
B	CYS216
B	LEU217
B	TYR220
B	ARG301

site_id	AD4
Number of Residues	6
Details	binding site for residue EDO B 407

Chain	Residue
B	ARG255
B	MET258
B	GLU263
B	ILE265
C	ASP134
C	LYS234

site_id	AD5
Number of Residues	15
Details	binding site for residue V5W C 401

Chain	Residue
C	ILE18
C	GLY19
C	ALA39
C	PHE91
C	GLU92
C	PHE93
C	MET94
C	ASP95
C	GLY96
C	LYS105
C	CYS146
C	LEU148
C	GLY161
C	GLY162
C	HOH526

site_id	AD6
Number of Residues	4
Details	binding site for residue EDO C 402

Chain	Residue
B	ASP251
B	PRO274
C	GLU171
C	LYS234

site_id	AD7
Number of Residues	3
Details	binding site for residue EDO C 403

Chain	Residue
B	LYS285
C	GLU13
C	EDO404

site_id	AD8
Number of Residues	4
Details	binding site for residue EDO C 404

Chain	Residue
C	CYS15
C	ARG28
C	ILE30
C	EDO403

site_id	AD9
Number of Residues	4
Details	binding site for residue EDO C 405

Chain	Residue
C	LYS41
C	VAL43
C	LEU59
C	GLU62

site_id	AE1
Number of Residues	15
Details	binding site for residue V5W D 401

Chain	Residue
D	PHE93
D	MET94
D	ASP95
D	GLY96
D	ALA97
D	LYS105
D	CYS146
D	LEU148
D	LYS152
D	GLY161
D	GLY162
D	ILE18
D	GLY19
D	ALA39
D	GLU92

site_id	AE2
Number of Residues	5
Details	binding site for residue EDO D 402

Chain	Residue
A	ASP134
D	ARG255
D	MET258
D	GLU263
D	ILE265

site_id	AE3
Number of Residues	1
Details	binding site for residue EDO D 403

Chain	Residue
D	ILE18

site_id	AE4
Number of Residues	3
Details	binding site for residue EDO D 404

Chain	Residue
D	LYS41
D	PHE48
D	GLU62

site_id	AE5
Number of Residues	4
Details	binding site for residue EDO D 405

Chain	Residue
D	CYS216
D	LEU217
D	TYR220
D	ARG301

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 2024-07-10

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