8GX2

The crystal structure of human CtsL in complex with 14c

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	PS00139
Number of Residues	12
Details	THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGqCGSCWAfSA

Chain	Residue	Details
A	GLN19-ALA30

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site_id	PS00639
Number of Residues	11
Details	THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. MDHGVLVVGYG

Chain	Residue	Details
A	MET161-GLY171

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

Chain	Residue	Details
A	TYR182-MET201

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000305|PubMed:9468501

Chain	Residue	Details
A	CYS25
B	CYS25

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site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE:

Chain	Residue	Details
A	HIS163
A	ASN187
B	HIS163
B	ASN187

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site_id	SWS_FT_FI3
Number of Residues	8
Details	SITE: Cleavage; by autolysis => ECO:0000269|PubMed:9468501

Chain	Residue	Details
A	PHE-7
A	GLN-6
A	TYR-1
A	GLU0
B	PHE-7
B	GLN-6
B	TYR-1
B	GLU0

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site_id	SWS_FT_FI4
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218

Chain	Residue	Details
A	ASN108
B	ASN108

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