1EF7

CRYSTAL STRUCTURE OF HUMAN CATHEPSIN X

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006508	biological_process	proteolysis
A	0008234	molecular_function	cysteine-type peptidase activity
B	0006508	biological_process	proteolysis
B	0008234	molecular_function	cysteine-type peptidase activity

Functional Information from PROSITE/UniProt

site_id	PS00640
Number of Residues	20
Details	THIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWIvRNSWgepWGerGWLrI

Chain	Residue	Details
A	TYR195-ILE214

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: ACT_SITE => ECO:0000305|PubMed:10656802, ECO:0000305|PubMed:10745011

Chain	Residue	Details
A	ALA41
A	SER190
A	GLY210
B	ALA41
B	SER190
B	GLY210

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site_id	SWS_FT_FI2
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218

Chain	Residue	Details
A	GLY133
B	GLY133

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site_id	SWS_FT_FI3
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	GLN173
B	GLN173

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 953

Chain	Residue	Details
A	TRP32	electrostatic stabiliser
A	ALA41	covalent catalysis, proton shuttle (general acid/base)
A	SER190	proton shuttle (general acid/base)
A	GLY210	electrostatic stabiliser, modifies pKa

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site_id	MCSA2
Number of Residues	4
Details	M-CSA 953

Chain	Residue	Details
B	TRP32	electrostatic stabiliser
B	ALA41	covalent catalysis, proton shuttle (general acid/base)
B	SER190	proton shuttle (general acid/base)
B	GLY210	electrostatic stabiliser, modifies pKa

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