6PX9

Crystal structure of procaspase-8 in complex with covalent small molecule inhibitor 63-R

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for Di-peptide 63R B 600 and CYS B 360

Chain	Residue
B	ARG260
B	ALA359
B	GLN361
B	VAL406
B	TRP420
E	ASP259
E	ASN261
B	ASN261
B	GLY262
B	LEU265
B	ASP266
B	SER316
B	HIS317
B	GLY318
B	GLN358

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	HIS304-GLY318

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

Chain	Residue	Details
A	LYS351-GLY362

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Active site: {"evidences":[{"source":"PubMed","id":"10508785","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O89110","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	6
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 818

Chain	Residue	Details
A	ARG258	electrostatic stabiliser
A	HIS317	proton acceptor, proton donor
A	GLY318	electrostatic stabiliser
A	CYS360	nucleofuge, nucleophile, proton acceptor, proton donor

---

site_id	MCSA2
Number of Residues	4
Details	M-CSA 818

Chain	Residue	Details
B	ARG258	electrostatic stabiliser
B	HIS317	proton acceptor, proton donor
B	GLY318	electrostatic stabiliser
B	CYS360	nucleofuge, nucleophile, proton acceptor, proton donor

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site_id	MCSA3
Number of Residues	4
Details	M-CSA 818

Chain	Residue	Details
C	ARG258	electrostatic stabiliser
C	HIS317	proton acceptor, proton donor
C	GLY318	electrostatic stabiliser
C	CYS360	nucleofuge, nucleophile, proton acceptor, proton donor

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site_id	MCSA4
Number of Residues	4
Details	M-CSA 818

Chain	Residue	Details
D	ARG258	electrostatic stabiliser
D	HIS317	proton acceptor, proton donor
D	GLY318	electrostatic stabiliser
D	CYS360	nucleofuge, nucleophile, proton acceptor, proton donor

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site_id	MCSA5
Number of Residues	4
Details	M-CSA 818

Chain	Residue	Details
E	ARG258	electrostatic stabiliser
E	HIS317	proton acceptor, proton donor
E	GLY318	electrostatic stabiliser
E	CYS360	nucleofuge, nucleophile, proton acceptor, proton donor

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site_id	MCSA6
Number of Residues	4
Details	M-CSA 818

Chain	Residue	Details
F	ARG258	electrostatic stabiliser
F	HIS317	proton acceptor, proton donor
F	GLY318	electrostatic stabiliser
F	CYS360	nucleofuge, nucleophile, proton acceptor, proton donor

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