8EG6

huCaspase-6 in complex with inhibitor 2a

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004197	molecular_function	cysteine-type endopeptidase activity
A	0006508	biological_process	proteolysis
A	0008234	molecular_function	cysteine-type peptidase activity
B	0004197	molecular_function	cysteine-type endopeptidase activity
B	0006508	biological_process	proteolysis
B	0008234	molecular_function	cysteine-type peptidase activity
C	0004197	molecular_function	cysteine-type endopeptidase activity
C	0006508	biological_process	proteolysis
C	0008234	molecular_function	cysteine-type peptidase activity
D	0004197	molecular_function	cysteine-type endopeptidase activity
D	0006508	biological_process	proteolysis
D	0008234	molecular_function	cysteine-type peptidase activity
E	0004197	molecular_function	cysteine-type endopeptidase activity
E	0006508	biological_process	proteolysis
E	0008234	molecular_function	cysteine-type peptidase activity
F	0004197	molecular_function	cysteine-type endopeptidase activity
F	0006508	biological_process	proteolysis
F	0008234	molecular_function	cysteine-type peptidase activity
G	0004197	molecular_function	cysteine-type endopeptidase activity
G	0006508	biological_process	proteolysis
G	0008234	molecular_function	cysteine-type peptidase activity
H	0004197	molecular_function	cysteine-type endopeptidase activity
H	0006508	biological_process	proteolysis
H	0008234	molecular_function	cysteine-type peptidase activity

Functional Information from PROSITE/UniProt

site_id	PS01121
Number of Residues	15
Details	CASPASE_HIS Caspase family histidine active site. HadadCfvCvFLSHG

Chain	Residue	Details
A	HIS108-GLY122

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site_id	PS01122
Number of Residues	12
Details	CASPASE_CYS Caspase family cysteine active site. KPKIFIIQACRG

Chain	Residue	Details
A	LYS154-GLY165

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Region: {"description":"Tri-arginine exosite","evidences":[{"source":"PubMed","id":"30420425","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	68
Details	Region: {"description":"130's region","evidences":[{"source":"PubMed","id":"28154009","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"evidences":[{"source":"PubMed","id":"30420425","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	4
Details	Active site: {"evidences":[{"source":"PubMed","id":"16123779","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19133298","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19694615","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20890311","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28864531","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30420425","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O08738","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine; by NUAK1 and AMPK","evidences":[{"source":"PubMed","id":"15273717","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22483120","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32029622","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	8
Details	Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"27911442","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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