5HVJ

Crystal structure of LIMK1 D460N mutant in complex with AMP-PNP

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ANP A 1000

Chain	Residue
A	GLU414
A	ILE416
A	THR420
A	LEU467

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGCFGQAIkVthretgev..........MVMK

Chain	Residue	Details
A	LEU345-LYS368

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000250

Chain	Residue	Details
A	ASN460
B	ASN460

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
B	LEU345
B	LYS368
A	LEU345
A	LYS368

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976

Chain	Residue	Details
A	SER337
B	SER337

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by ROCK1 and PAK1 => ECO:0000269|PubMed:10559936, ECO:0000269|PubMed:10652353, ECO:0000269|PubMed:15660133, ECO:0000269|PubMed:23633677

Chain	Residue	Details
A	THR508
B	THR508

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