5DRB

Crystal structure of WNK1 in complex with WNK463

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	19
Details	binding site for residue 5FJ A 501

Chain	Residue
A	GLY228
A	THR301
A	GLU302
A	MET304
A	PHE356
A	ASP368
A	LEU369
A	GLY370
A	HOH652
A	HOH682
A	HOH695
A	VAL235
A	ALA248
A	CYS250
A	PHE265
A	ALA269
A	LEU272
A	PHE283
A	LEU299

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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. IiHrDLKcdNIFI

Chain	Residue	Details
A	ILE345-ILE357

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:10828064, ECO:0000305|PubMed:16083423

Chain	Residue	Details
A	ASP368

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q9H4A3

Chain	Residue	Details
A	SER231
A	THR301
A	LYS351

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305|PubMed:24803536, ECO:0007744|PDB:4Q2A

Chain	Residue	Details
A	PHE283
A	LEU299
A	LEU369
A	LEU371

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:12374799

Chain	Residue	Details
A	SER378

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:12374799, ECO:0000269|PubMed:22544747

Chain	Residue	Details
A	ALA382

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