7MP8

Crystal structure of the cytosolic domain of Tribolium castaneum PINK1 in the non-phosphorylated state

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	2
Details	binding site for residue SO4 A 601

Chain	Residue
A	ARG296
A	HOH701

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site_id	AC2
Number of Residues	2
Details	binding site for residue SO4 A 602

Chain	Residue
A	ARG134
A	LYS551

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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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site_id	PS00373
Number of Residues	24
Details	GART Phosphoribosylglycinamide formyltransferase active site. GlSLpYTsAeMDkGgnTalmapeI

Chain	Residue	Details
A	GLY370-ILE393

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	449
Details	TOPO_DOM: Cytoplasmic => ECO:0000305

Chain	Residue	Details
A	THR121-ASP570

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:29991771

Chain	Residue	Details
A	ASP337

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:29991771, ECO:0007744|PDB:5YJ9

Chain	Residue	Details
A	LYS196

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site_id	SWS_FT_FI4
Number of Residues	7
Details	BINDING: BINDING => ECO:0000269|PubMed:29991771, ECO:0007744|PDB:5YJ9

Chain	Residue	Details
A	GLU217
A	LYS295
A	TYR297
A	ASN300
A	ASP341
A	ASN342
A	ASP359

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site_id	SWS_FT_FI5
Number of Residues	1
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	SER205

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:29991771

Chain	Residue	Details
A	SER377

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:29991771

Chain	Residue	Details
A	THR386

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site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:29991771

Chain	Residue	Details
A	THR530

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