3MII

Crystal structure of Y0R391Cp/HSP33 from Saccharomyces cerevisiae

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000932	cellular_component	P-body
A	0005575	cellular_component	cellular_component
A	0005737	cellular_component	cytoplasm
A	0006457	biological_process	protein folding
A	0016829	molecular_function	lyase activity
A	0019172	molecular_function	glyoxalase III activity
A	0019243	biological_process	obsolete methylglyoxal catabolic process to pyruvate via (R)-S-lactoyl-glutathione
A	0019249	biological_process	lactate biosynthetic process
A	0031669	biological_process	cellular response to nutrient levels
A	0044183	molecular_function	protein folding chaperone
B	0000932	cellular_component	P-body
B	0005575	cellular_component	cellular_component
B	0005737	cellular_component	cytoplasm
B	0006457	biological_process	protein folding
B	0016829	molecular_function	lyase activity
B	0019172	molecular_function	glyoxalase III activity
B	0019243	biological_process	obsolete methylglyoxal catabolic process to pyruvate via (R)-S-lactoyl-glutathione
B	0019249	biological_process	lactate biosynthetic process
B	0031669	biological_process	cellular response to nutrient levels
B	0044183	molecular_function	protein folding chaperone

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PGE A 238

Chain	Residue
A	TYR60
A	HIS108
A	CSO138

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 238

Chain	Residue
B	LYS118
B	ASP122
B	GLY146
B	ILE148

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site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 239

Chain	Residue
A	ARG182
B	ARG154

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site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PGE B 240

Chain	Residue
B	TYR60
B	HIS108
B	PHE165

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"evidences":[{"source":"PubMed","id":"21139195","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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