3P4U

Crystal structure of active caspase-6 in complex with Ac-VEID-CHO inhibitor

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR CHAIN E OF AC-VEID-CHO

Chain	Residue
A	ARG64
B	ARG220
B	GLU221
B	THR222
B	CAS264
A	ARG65
A	HIS121
A	GLY122
A	GLN161
A	CYS163
B	TYR217
B	SER218
B	HIS219

---

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR CHAIN F OF AC-VEID-CHO

Chain	Residue
C	ARG64
C	HIS121
C	GLN161
C	CYS163
C	HOH311
D	TYR217
D	SER218
D	HIS219
D	ARG220
D	GLU221
D	THR222
D	CAS264
D	HOH422

---

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

---

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	4
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	34
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	2
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	2
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	2
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	2
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	4
Details	Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"27911442","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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