6BWK

Crystal structure of the human MLKL pseudokinase domain T357E/S358E mutant

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	3
Details	binding site for residue GOL A 501

Chain	Residue
A	LYS230
A	ALA348
A	GLY349

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site_id	AC2
Number of Residues	5
Details	binding site for residue GOL A 502

Chain	Residue
A	ARG210
A	CYS286
A	GLY289
A	LEU338
A	HOH601

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site_id	AC3
Number of Residues	3
Details	binding site for residue GOL A 503

Chain	Residue
A	ARG224
A	ARG315
A	GLU221

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site_id	AC4
Number of Residues	4
Details	binding site for residue GOL A 504

Chain	Residue
A	HIS321
A	PRO326
A	LEU328
A	VAL391

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU209

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	LYS230

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by RIPK3 => ECO:0000269|PubMed:22265413

Chain	Residue	Details
A	GLU357

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine; by RIPK3 => ECO:0000269|PubMed:22265413, ECO:0000269|PubMed:29883610

Chain	Residue	Details
A	GLU358

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine; by RIPK3 => ECO:0000250|UniProtKB:Q9D2Y4

Chain	Residue	Details
A	SER360

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