6VNO

Cryo-EM structure of the C-terminal half of the Parkinson's Disease-linked protein Leucine Rich Repeat Kinase 2 (LRRK2)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0005525	molecular_function	GTP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue GDP A 2601

Chain	Residue
A	TPO1343
A	ASN1489
A	ALA1490
A	THR1491
A	MG2602
A	GLY1344
A	SER1345
A	GLY1346
A	LYS1347
A	THR1348
A	THR1349
A	HIS1453
A	ASP1455

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site_id	AC2
Number of Residues	2
Details	binding site for residue MG A 2602

Chain	Residue
A	THR1348
A	GDP2601

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	22
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGDGSFGSVYrAayegee............VAVK

Chain	Residue	Details
A	LEU1885-LYS1906

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

Chain	Residue	Details
A	ILE1990-LEU2002

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site_id	PS00626
Number of Residues	11
Details	RCC1_2 Regulator of chromosome condensation (RCC1) signature 2. IGTGgGHILLL

Chain	Residue	Details
A	ILE2427-LEU2437

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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:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP1994

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00758, ECO:0000269|PubMed:18230735

Chain	Residue	Details
A	GLY1341

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LYS1906
A	LEU1885

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site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00758

Chain	Residue	Details
A	ASN2295
A	GLU2098

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:28202711

Chain	Residue	Details
A	SER1444

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