5YJ9

Crystal structure of Tribolium castaneum PINK1 kinase domain in complex with AMP-PNP

Functional Information from GO Data

Chain	GOid	namespace	contents
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	18
Details	binding site for residue ANP D 601

Chain	Residue
D	ALA169
D	ASN342
D	LEU344
D	ASP359
D	LYS446
D	ASP449
D	MG602
D	MG603
D	HOH701
D	HOH702
D	ALA194
D	LYS196
D	GLU217
D	MSE294
D	LYS295
D	TYR297
D	ASN300
D	ASP341

---

site_id	AC2
Number of Residues	4
Details	binding site for residue MG D 602

Chain	Residue
D	GLU217
D	ASP359
D	ANP601
D	HOH703

---

site_id	AC3
Number of Residues	5
Details	binding site for residue MG D 603

Chain	Residue
D	ASN342
D	ASP359
D	ANP601
D	HOH701
D	HOH702

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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
D	ILE333-LEU345

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:29991771

Chain	Residue	Details
D	ASP337

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:29991771, ECO:0007744|PDB:5YJ9

Chain	Residue	Details
D	LYS196

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site_id	SWS_FT_FI3
Number of Residues	7
Details	BINDING: BINDING => ECO:0000269|PubMed:29991771, ECO:0007744|PDB:5YJ9

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

---

site_id	SWS_FT_FI4
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
D	ASP205

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:29991771

Chain	Residue	Details
D	ASP377

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

Chain	Residue	Details
D	GLU386

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

Chain	Residue	Details
D	GLU530

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