5OAT

PINK1 structure

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	binding site for residue MG A 601

Chain	Residue
A	ASP359

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site_id	AC2
Number of Residues	2
Details	binding site for residue MG C 601

Chain	Residue
B	ASP359
C	ASP229

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site_id	AC3
Number of Residues	1
Details	binding site for residue MG E 601

Chain	Residue
E	ASP229

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site_id	AC4
Number of Residues	1
Details	binding site for residue MG E 602

Chain	Residue
E	ASP359

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site_id	AC5
Number of Residues	2
Details	binding site for residue MG F 601

Chain	Residue
D	ASP359
F	ASP229

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE333-LEU345

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:29991771

Chain	Residue	Details
A	THR347
B	THR347
C	THR347
D	THR347
E	THR347
F	THR347

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:29991771, ECO:0007744|PDB:5YJ9

Chain	Residue	Details
A	LYS196
B	LYS196
C	LYS196
D	LYS196
E	LYS196
F	LYS196

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site_id	SWS_FT_FI3
Number of Residues	42
Details	BINDING: BINDING => ECO:0000269|PubMed:29991771, ECO:0007744|PDB:5YJ9

Chain	Residue	Details
A	GLU217
B	THR307
B	SER310
B	GLU351
B	SER352
B	ASN369
C	GLU217
C	LEU305
C	THR307
C	SER310
C	GLU351
A	LEU305
C	SER352
C	ASN369
D	GLU217
D	LEU305
D	THR307
D	SER310
D	GLU351
D	SER352
D	ASN369
E	GLU217
A	THR307
E	LEU305
E	THR307
E	SER310
E	GLU351
E	SER352
E	ASN369
F	GLU217
F	LEU305
F	THR307
F	SER310
A	SER310
F	GLU351
F	SER352
F	ASN369
A	GLU351
A	SER352
A	ASN369
B	GLU217
B	LEU305

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:22645651, ECO:0000269|PubMed:28980524, ECO:0000269|PubMed:29475881, ECO:0000269|PubMed:29991771

Chain	Residue	Details
A	GLU205
B	GLU205
C	GLU205
D	GLU205
E	GLU205
F	GLU205

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:29991771

Chain	Residue	Details
A	ALA387
B	ALA387
C	ALA387
D	ALA387
E	ALA387
F	ALA387

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site_id	SWS_FT_FI6
Number of Residues	6
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:29991771

Chain	Residue	Details
A	GLN396
B	GLN396
C	GLN396
D	GLN396
E	GLN396
F	GLN396

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site_id	SWS_FT_FI7
Number of Residues	6
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:29991771

Chain	Residue	Details
A	TYR540
B	TYR540
C	TYR540
D	TYR540
E	TYR540
F	TYR540

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