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	Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by ROCK1 and PAK1","evidences":[{"source":"PubMed","id":"10559936","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10652353","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15660133","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23633677","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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