4HQR

Crystal Structure of mutant form of Caspase-7

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR CHAIN E OF AC-ASP-GLU-VAL-ASP-ALDEHYDE

Chain	Residue
A	ARG87
A	SER234
A	PRO235
A	HIS144
A	GLY145
A	GLN184
A	CYS186
A	TYR230
A	SER231
A	TRP232
A	ARG233

---

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR CHAIN F OF AC-ASP-GLU-VAL-ASP-ALDEHYDE

Chain	Residue
B	ARG87
B	HIS144
B	GLY145
B	GLN184
B	CYS186
B	SER231
B	TRP232
B	ARG233
B	SER234
B	PRO235
B	TRP240
B	SER275
B	GLN276

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	HIS131-GLY145

---

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

Chain	Residue	Details
A	LYS177-GLY188

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	22
Details	Region: {"description":"Loop L1","evidences":[{"source":"PubMed","id":"23897474","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	24
Details	Region: {"description":"Loop L3","evidences":[{"source":"PubMed","id":"23897474","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PubMed","id":"15314233","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PubMed","id":"11701129","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15314233","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16916640","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Site: {"description":"Involved in allosteric regulation","evidences":[{"source":"PubMed","id":"15314233","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19581639","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine; by PAK2","evidences":[{"source":"PubMed","id":"21555521","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27889207","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"(Microbial infection) ADP-riboxanated arginine","evidences":[{"source":"PubMed","id":"35338844","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35446120","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"PubMed","id":"21555521","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27889207","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	9
Details	Region: {"description":"Loop L2","evidences":[{"source":"PubMed","id":"23897474","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	14
Details	Region: {"description":"Loop L4","evidences":[{"source":"PubMed","id":"23897474","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

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