7T4M

Structure of dodecameric unphosphorylated Pediculus humanus (Ph) PINK1 D357A mutant

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
E	0004672	molecular_function	protein kinase activity
E	0005524	molecular_function	ATP binding
E	0006468	biological_process	protein phosphorylation
F	0004672	molecular_function	protein kinase activity
F	0005524	molecular_function	ATP binding
F	0006468	biological_process	protein phosphorylation
G	0004672	molecular_function	protein kinase activity
G	0005524	molecular_function	ATP binding
G	0006468	biological_process	protein phosphorylation
H	0004672	molecular_function	protein kinase activity
H	0005524	molecular_function	ATP binding
H	0006468	biological_process	protein phosphorylation
I	0004672	molecular_function	protein kinase activity
I	0005524	molecular_function	ATP binding
I	0006468	biological_process	protein phosphorylation
J	0004672	molecular_function	protein kinase activity
J	0005524	molecular_function	ATP binding
J	0006468	biological_process	protein phosphorylation
K	0004672	molecular_function	protein kinase activity
K	0005524	molecular_function	ATP binding
K	0006468	biological_process	protein phosphorylation
L	0004672	molecular_function	protein kinase activity
L	0005524	molecular_function	ATP binding
L	0006468	biological_process	protein phosphorylation

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE330-VAL342

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5472
Details	TOPO_DOM: Cytoplasmic => ECO:0000305

Chain	Residue	Details
A	THR119-ASN575
J	THR119-ASN575
K	THR119-ASN575
L	THR119-ASN575
B	THR119-ASN575
C	THR119-ASN575
D	THR119-ASN575
E	THR119-ASN575
F	THR119-ASN575
G	THR119-ASN575
H	THR119-ASN575
I	THR119-ASN575

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site_id	SWS_FT_FI2
Number of Residues	12
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ASP334
J	ASP334
K	ASP334
L	ASP334
B	ASP334
C	ASP334
D	ASP334
E	ASP334
F	ASP334
G	ASP334
H	ASP334
I	ASP334

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site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LYS193
J	LYS193
K	LYS193
L	LYS193
B	LYS193
C	LYS193
D	LYS193
E	LYS193
F	LYS193
G	LYS193
H	LYS193
I	LYS193

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site_id	SWS_FT_FI4
Number of Residues	36
Details	BINDING: BINDING => ECO:0000250|UniProtKB:D6WMX4

Chain	Residue	Details
A	GLU214
D	GLU214
D	ASN339
D	ALA357
E	GLU214
E	ASN339
E	ALA357
F	GLU214
F	ASN339
F	ALA357
G	GLU214
A	ASN339
G	ASN339
G	ALA357
H	GLU214
H	ASN339
H	ALA357
I	GLU214
I	ASN339
I	ALA357
J	GLU214
J	ASN339
A	ALA357
J	ALA357
K	GLU214
K	ASN339
K	ALA357
L	GLU214
L	ASN339
L	ALA357
B	GLU214
B	ASN339
B	ALA357
C	GLU214
C	ASN339
C	ALA357

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site_id	SWS_FT_FI5
Number of Residues	24
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:29160309

Chain	Residue	Details
A	SER202
E	SER204
F	SER202
F	SER204
G	SER202
G	SER204
H	SER202
H	SER204
I	SER202
I	SER204
J	SER202
A	SER204
J	SER204
K	SER202
K	SER204
L	SER202
L	SER204
B	SER202
B	SER204
C	SER202
C	SER204
D	SER202
D	SER204
E	SER202

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site_id	SWS_FT_FI6
Number of Residues	12
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:29160309

Chain	Residue	Details
A	THR305
J	THR305
K	THR305
L	THR305
B	THR305
C	THR305
D	THR305
E	THR305
F	THR305
G	THR305
H	THR305
I	THR305

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