1QTN

CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-8 WITH THE TETRAPEPTIDE INHIBITOR ACE-IETD-ALDEHYDE

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	9
Details	BINDING SITE FOR RESIDUE DTD B 505

Chain	Residue
A	TYR334
A	THR337
B	GLU396
B	PHE399
B	LEU401
B	THR469
B	HOH657
B	HOH681
B	HOH690

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DTD A 506

Chain	Residue
A	LYS231
A	PRO232
A	HIS278
A	GLU290
A	GLU294
A	HOH714

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site_id	AC3
Number of Residues	21
Details	BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE

Chain	Residue
A	ARG260
A	HIS317
A	GLY318
A	GLN358
A	CYS360
A	HOH694
B	SER411
B	TYR412
B	ARG413
B	PRO415
B	TRP420
B	HOH665
C	HOH632
C	HOH675
C	HOH677
C	HOH759
C	HOH797
C	HOH878
C	HOH890
C	HOH909
C	HOH914

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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	1
Details	MOD_RES: Phosphoserine; by CDK1 => ECO:0000269|PubMed:20937773

Chain	Residue	Details
B	SER387
A	CYS360

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: (Microbial infection) ADP-riboxanated arginine => ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35446120

Chain	Residue	Details
B	ARG413

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site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Cleavage; by CASP6 => ECO:0000269|PubMed:22858542

Chain	Residue	Details
A	ASP374

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O89110

Chain	Residue	Details
A	SER211

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O89110

Chain	Residue	Details
A	LYS224

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455

Chain	Residue	Details
A	TYR334

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 10508785

Chain	Residue	Details
A	GLY350
A	HIS317
A	CYS360
A	ARG258

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site_id	MCSA1
Number of Residues
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

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