3MWZ

Crystal structure of the selenomethionine derivative of the L 22,47,100 M mutant of sialostatin L2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004869	molecular_function	cysteine-type endopeptidase inhibitor activity
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0031982	cellular_component	vesicle
A	2000117	biological_process	negative regulation of cysteine-type endopeptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 116

Chain	Residue
A	GLY7
A	ARG61
A	HOH159
A	HOH230

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Functional Information from PROSITE/UniProt

site_id	PS00287
Number of Residues	14
Details	CYSTATIN Cysteine proteases inhibitors signature. TQTVAGTNYrLTLK

Chain	Residue	Details
A	THR52-LYS65

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	SITE: Reactive site => ECO:0000250|UniProtKB:P01040

Chain	Residue	Details
A	GLY7

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