Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1F9E

CASPASE-8 SPECIFICITY PROBED AT SUBSITE S4: CRYSTAL STRUCTURE OF THE CASPASE-8-Z-DEVD-CHO

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	13
Details	BINDING SITE FOR CHAIN Q OF (PHQ)DEVD

Chain	Residue
A	ARG179
B	PRO343
B	ALA344
B	THR347
B	TRP348
A	HIS237
A	GLY238
A	GLN283
A	CYS285
B	SER339
B	TYR340
B	ARG341
B	ASN342

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR CHAIN R OF (PHQ)DEVD

Chain	Residue
C	ARG179
C	HIS237
C	GLY238
C	GLN283
C	CYS285
D	SER339
D	ARG341
D	ASN342
D	PRO343
D	ALA344
D	TRP348
D	ASP381
D	LYS381
F	ALA344

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR CHAIN S OF (PHQ)DEVD

Chain	Residue
E	ARG177
E	ARG179
E	HIS237
E	GLN283
E	CYS285
F	SER339
F	TYR340
F	ARG341
F	ASN342
F	PRO343
F	TRP348
F	LYS381

site_id	AC4
Number of Residues	17
Details	BINDING SITE FOR CHAIN T OF (PHQ)DEVD

Chain	Residue
A	LEU184
A	GLY187
A	THR191
G	ARG177
G	ARG179
G	HIS237
G	GLY238
G	GLN283
G	CYS285
H	SER339
H	TYR340
H	ARG341
H	ASN342
H	PRO343
H	ALA344
H	THR347
H	TRP348

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR CHAIN U OF (PHQ)DEVD

Chain	Residue
I	ARG177
I	ARG179
I	HIS237
I	GLY238
I	GLN283
I	CYS285
J	VAL338
J	SER339
J	TYR340
J	ARG341
J	ASN342
J	PRO343
J	TRP348

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR CHAIN V OF (PHQ)DEVD

Chain	Residue
K	ARG177
K	ARG179
K	HIS237
K	GLY238
K	GLN283
K	CYS285
L	SER339
L	TYR340
L	ARG341
L	ASN342
L	PRO343
L	TRP348
L	LYS381

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	12
Details	Active site: {"evidences":[{"source":"PubMed","id":"10508785","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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

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

site_id	SWS_FT_FI4
Number of Residues	6
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

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	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	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	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
D	CYS354	electrostatic stabiliser

site_id	MCSA3
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	MCSA4
Number of Residues
Details	M-CSA 818

Chain	Residue	Details
J	CYS354	electrostatic stabiliser

site_id	MCSA5
Number of Residues
Details	M-CSA 818

Chain

Residue

Details

site_id	MCSA6
Number of Residues
Details	M-CSA 818

Chain

Residue

Details

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