3KSE

Unreduced cathepsin L in complex with stefin A

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
C	0006508	biological_process	proteolysis
C	0008234	molecular_function	cysteine-type peptidase activity
D	0001533	cellular_component	cornified envelope
D	0002020	molecular_function	protease binding
D	0004866	molecular_function	endopeptidase inhibitor activity
D	0004869	molecular_function	cysteine-type endopeptidase inhibitor activity
D	0005515	molecular_function	protein binding
D	0005615	cellular_component	extracellular space
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0007155	biological_process	cell adhesion
D	0010466	biological_process	negative regulation of peptidase activity
D	0018149	biological_process	peptide cross-linking
D	0030216	biological_process	keratinocyte differentiation
D	0045861	biological_process	negative regulation of proteolysis
D	0098609	biological_process	cell-cell adhesion
D	1904090	cellular_component	peptidase inhibitor complex
E	0001533	cellular_component	cornified envelope
E	0002020	molecular_function	protease binding
E	0004866	molecular_function	endopeptidase inhibitor activity
E	0004869	molecular_function	cysteine-type endopeptidase inhibitor activity
E	0005515	molecular_function	protein binding
E	0005615	cellular_component	extracellular space
E	0005654	cellular_component	nucleoplasm
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0007155	biological_process	cell adhesion
E	0010466	biological_process	negative regulation of peptidase activity
E	0018149	biological_process	peptide cross-linking
E	0030216	biological_process	keratinocyte differentiation
E	0045861	biological_process	negative regulation of proteolysis
E	0098609	biological_process	cell-cell adhesion
E	1904090	cellular_component	peptidase inhibitor complex
F	0001533	cellular_component	cornified envelope
F	0002020	molecular_function	protease binding
F	0004866	molecular_function	endopeptidase inhibitor activity
F	0004869	molecular_function	cysteine-type endopeptidase inhibitor activity
F	0005515	molecular_function	protein binding
F	0005615	cellular_component	extracellular space
F	0005654	cellular_component	nucleoplasm
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0007155	biological_process	cell adhesion
F	0010466	biological_process	negative regulation of peptidase activity
F	0018149	biological_process	peptide cross-linking
F	0030216	biological_process	keratinocyte differentiation
F	0045861	biological_process	negative regulation of proteolysis
F	0098609	biological_process	cell-cell adhesion
F	1904090	cellular_component	peptidase inhibitor complex

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

Chain	Residue	Details
D	THR45-ARG58

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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	3
Details	SITE: Reactive site

Chain	Residue	Details
D	GLY4
E	GLY4
F	GLY4

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site_id	SWS_FT_FI2
Number of Residues	3
Details	MOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P01039

Chain	Residue	Details
D	MET1
E	MET1
F	MET1
B	ASN187
C	HIS163
C	ASN187

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site_id	SWS_FT_FI3
Number of Residues	3
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
C	ASN108

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