Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1QDU

CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-8 WITH THE TRIPEPTIDE KETONE INHIBITOR ZEVD-DCBMK

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
I	0004197	molecular_function	cysteine-type endopeptidase activity
I	0006508	biological_process	proteolysis
I	0008234	molecular_function	cysteine-type peptidase activity
J	0004197	molecular_function	cysteine-type endopeptidase activity
J	0006508	biological_process	proteolysis
J	0008234	molecular_function	cysteine-type peptidase activity
K	0004197	molecular_function	cysteine-type endopeptidase activity
K	0006508	biological_process	proteolysis
K	0008234	molecular_function	cysteine-type peptidase activity
L	0004197	molecular_function	cysteine-type endopeptidase activity
L	0006508	biological_process	proteolysis
L	0008234	molecular_function	cysteine-type peptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR CHAIN T OF PHQ-GLU-VAL-ASP-DICHLOROMETHYLKETONE INHIBITOR

Chain	Residue
A	ARG179
A	HIS237
A	GLY238
A	CYS285
B	SER339
B	TYR340
B	ARG341
B	PRO343

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR CHAIN U OF PHQ-GLU-VAL-ASP-DICHLOROMETHYLKETONE INHIBITOR

Chain	Residue
C	ARG179
C	HIS237
C	GLY238
C	GLN283
C	CYS285
D	SER339
D	TYR340
D	ARG341
D	THR347
C	HOH54

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR CHAIN V OF PHQ-GLU-VAL-ASP-DICHLOROMETHYLKETONE INHIBITOR

Chain	Residue
E	ARG177
E	ARG179
E	HIS237
E	GLY238
E	GLN283
E	CYS285
F	SER339
F	TYR340
F	ARG341
V	HOH103
V	HOH116

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR CHAIN W OF PHQ-GLU-VAL-ASP-DICHLOROMETHYLKETONE INHIBITOR

Chain	Residue
G	ARG179
G	HIS237
G	GLY238
G	GLN283
G	CYS285
H	SER339
H	TYR340
H	ARG341
H	PRO343

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR CHAIN X OF PHQ-GLU-VAL-ASP-DICHLOROMETHYLKETONE INHIBITOR

Chain	Residue
I	ARG179
I	HIS237
I	GLY238
I	GLN283
I	CYS285
J	SER339
J	TYR340
J	ARG341
J	PRO343

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR CHAIN Y OF PHQ-GLU-VAL-ASP-DICHLOROMETHYLKETONE INHIBITOR

Chain	Residue
K	ARG179
K	HIS237
K	GLY238
K	GLN283
K	CYS285
L	SER339
L	TYR340
L	ARG341
Y	HOH104

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	HIS224-GLY238

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

Chain	Residue	Details
A	LYS276-GLY287

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	MOD_RES: (Microbial infection) ADP-riboxanated arginine => ECO:0000269\|PubMed:35338844, ECO:0000269\|PubMed:35446120

Chain	Residue	Details
B	ARG341
I	CYS285
K	HIS237
K	CYS285
D	ARG341
F	ARG341
H	ARG341
J	ARG341
L	ARG341
G	HIS237
G	CYS285
I	HIS237

site_id	SWS_FT_FI2
Number of Residues	6
Details	SITE: Cleavage; by CASP6 => ECO:0000269\|PubMed:22858542

Chain	Residue	Details
A	ASP299
C	ASP299
E	ASP299
G	ASP299
I	ASP299
K	ASP299

site_id	SWS_FT_FI3
Number of Residues	6
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:O89110

Chain	Residue	Details
A	LYS151
C	LYS151
E	LYS151
G	LYS151
I	LYS151
K	LYS151

site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:15592455

Chain	Residue	Details
A	TYR259
C	TYR259
E	TYR259
G	TYR259
I	TYR259
K	TYR259

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1nw9

Chain	Residue	Details
A	GLY238
A	ARG177
A	CYS285
A	HIS237

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1nw9

Chain	Residue	Details
C	GLY238
C	ARG177
C	CYS285
C	HIS237

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1nw9

Chain	Residue	Details
E	GLY238
E	ARG177
E	CYS285
E	HIS237

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1nw9

Chain	Residue	Details
G	GLY238
G	ARG177
G	CYS285
G	HIS237

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1nw9

Chain	Residue	Details
I	GLY238
I	ARG177
I	CYS285
I	HIS237

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1nw9

Chain	Residue	Details
K	GLY238
K	ARG177
K	CYS285
K	HIS237

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1nw9

Chain	Residue	Details
A	ARG177
A	CYS285
A	HIS237
A	GLY275

site_id	CSA8
Number of Residues	4
Details	Annotated By Reference To The Literature 1nw9

Chain	Residue	Details
C	ARG177
C	CYS285
C	HIS237
C	GLY275

site_id	CSA9
Number of Residues	4
Details	Annotated By Reference To The Literature 1nw9

Chain	Residue	Details
E	ARG177
E	CYS285
E	HIS237
E	GLY275

site_id	CSA10
Number of Residues	4
Details	Annotated By Reference To The Literature 1nw9

Chain	Residue	Details
G	ARG177
G	CYS285
G	HIS237
G	GLY275

site_id	CSA11
Number of Residues	4
Details	Annotated By Reference To The Literature 1nw9

Chain	Residue	Details
I	ARG177
I	CYS285
I	HIS237
I	GLY275

site_id	CSA12
Number of Residues	4
Details	Annotated By Reference To The Literature 1nw9

Chain	Residue	Details
K	ARG177
K	CYS285
K	HIS237
K	GLY275

site_id	CSA13
Number of Residues	3
Details	Annotated By Reference To The Literature 1nw9

Chain	Residue	Details
A	CYS285
A	HIS237
A	GLY238

site_id	CSA14
Number of Residues	3
Details	Annotated By Reference To The Literature 1nw9

Chain	Residue	Details
C	CYS285
C	HIS237
C	GLY238

site_id	CSA15
Number of Residues	3
Details	Annotated By Reference To The Literature 1nw9

Chain	Residue	Details
E	CYS285
E	HIS237
E	GLY238

site_id	CSA16
Number of Residues	3
Details	Annotated By Reference To The Literature 1nw9

Chain	Residue	Details
G	CYS285
G	HIS237
G	GLY238

site_id	CSA17
Number of Residues	3
Details	Annotated By Reference To The Literature 1nw9

Chain	Residue	Details
I	CYS285
I	HIS237
I	GLY238

site_id	CSA18
Number of Residues	3
Details	Annotated By Reference To The Literature 1nw9

Chain	Residue	Details
K	CYS285
K	HIS237
K	GLY238

site_id	MCSA1
Number of Residues
Details	M-CSA 818

Chain	Residue	Details
A	ARG177	electrostatic stabiliser
A	HIS237	proton acceptor, proton donor
A	GLY238	electrostatic stabiliser
A	CYS285	nucleofuge, nucleophile, proton acceptor, proton donor

site_id	MCSA2
Number of Residues
Details	M-CSA 818

Chain	Residue	Details
C	ARG177	electrostatic stabiliser
C	HIS237	proton acceptor, proton donor
C	GLY238	electrostatic stabiliser
C	CYS285	nucleofuge, nucleophile, proton acceptor, proton donor

site_id	MCSA3
Number of Residues
Details	M-CSA 818

Chain	Residue	Details
E	ARG177	electrostatic stabiliser
E	HIS237	proton acceptor, proton donor
E	GLY238	electrostatic stabiliser
E	CYS285	nucleofuge, nucleophile, proton acceptor, proton donor

site_id	MCSA4
Number of Residues
Details	M-CSA 818

Chain	Residue	Details
G	ARG177	electrostatic stabiliser
G	HIS237	proton acceptor, proton donor
G	GLY238	electrostatic stabiliser
G	CYS285	nucleofuge, nucleophile, proton acceptor, proton donor

site_id	MCSA5
Number of Residues
Details	M-CSA 818

Chain	Residue	Details
I	ARG177	electrostatic stabiliser
I	HIS237	proton acceptor, proton donor
I	GLY238	electrostatic stabiliser
I	CYS285	nucleofuge, nucleophile, proton acceptor, proton donor

site_id	MCSA6
Number of Residues
Details	M-CSA 818

Chain	Residue	Details
K	ARG177	electrostatic stabiliser
K	HIS237	proton acceptor, proton donor
K	GLY238	electrostatic stabiliser
K	CYS285	nucleofuge, nucleophile, proton acceptor, proton donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)