Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1F1J

CRYSTAL STRUCTURE OF CASPASE-7 IN COMPLEX WITH ACETYL-ASP-GLU-VAL-ASP-CHO

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003723	molecular_function	RNA binding
A	0004190	molecular_function	aspartic-type endopeptidase activity
A	0004197	molecular_function	cysteine-type endopeptidase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006508	biological_process	proteolysis
A	0006915	biological_process	apoptotic process
A	0007507	biological_process	heart development
A	0008233	molecular_function	peptidase activity
A	0008234	molecular_function	cysteine-type peptidase activity
A	0009411	biological_process	response to UV
A	0016485	biological_process	protein processing
A	0030163	biological_process	protein catabolic process
A	0042742	biological_process	defense response to bacterium
A	0043525	biological_process	positive regulation of neuron apoptotic process
A	0044346	biological_process	fibroblast apoptotic process
A	0051146	biological_process	striated muscle cell differentiation
A	0051402	biological_process	neuron apoptotic process
A	0051604	biological_process	protein maturation
A	0070227	biological_process	lymphocyte apoptotic process
A	0071222	biological_process	cellular response to lipopolysaccharide
A	0071887	biological_process	leukocyte apoptotic process
A	0072734	biological_process	cellular response to staurosporine
A	0097153	molecular_function	cysteine-type endopeptidase activity involved in apoptotic process
A	0097194	biological_process	execution phase of apoptosis
A	0097200	molecular_function	cysteine-type endopeptidase activity involved in execution phase of apoptosis
A	1905686	biological_process	positive regulation of plasma membrane repair
B	0003723	molecular_function	RNA binding
B	0004190	molecular_function	aspartic-type endopeptidase activity
B	0004197	molecular_function	cysteine-type endopeptidase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006508	biological_process	proteolysis
B	0006915	biological_process	apoptotic process
B	0007507	biological_process	heart development
B	0008233	molecular_function	peptidase activity
B	0008234	molecular_function	cysteine-type peptidase activity
B	0009411	biological_process	response to UV
B	0016485	biological_process	protein processing
B	0030163	biological_process	protein catabolic process
B	0042742	biological_process	defense response to bacterium
B	0043525	biological_process	positive regulation of neuron apoptotic process
B	0044346	biological_process	fibroblast apoptotic process
B	0051146	biological_process	striated muscle cell differentiation
B	0051402	biological_process	neuron apoptotic process
B	0051604	biological_process	protein maturation
B	0070227	biological_process	lymphocyte apoptotic process
B	0071222	biological_process	cellular response to lipopolysaccharide
B	0071887	biological_process	leukocyte apoptotic process
B	0072734	biological_process	cellular response to staurosporine
B	0097153	molecular_function	cysteine-type endopeptidase activity involved in apoptotic process
B	0097194	biological_process	execution phase of apoptosis
B	0097200	molecular_function	cysteine-type endopeptidase activity involved in execution phase of apoptosis
B	1905686	biological_process	positive regulation of plasma membrane repair

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 1201

Chain	Residue
A	LYS76
A	ASN88
A	GLY89
A	THR90
A	ASP91
A	LYS92
A	HOH1136

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 1202

Chain	Residue
B	THR390
B	ASP391
B	LYS392
B	LYS399
B	HOH775
B	LYS376
B	GLY389

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR CHAIN C OF ACE-ASP-GLU-VAL-ASP-CHO

Chain	Residue
A	ARG87
A	ASN88
A	SER143
A	HIS144
A	GLY145
A	GLN184
A	CYS186
A	TYR230
A	SER231
A	TRP232
A	ARG233
A	SER234
A	PRO235
A	SER275
A	GLN276
C	HOH921
C	HOH1130

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR CHAIN D OF ACE-ASP-GLU-VAL-ASP-CHO

Chain	Residue
B	ARG387
B	HIS444
B	GLY445
B	GLN484
B	CYS486
B	SER531
B	TRP532
B	ARG533
B	SER534
B	PRO535
B	SER575
B	GLN576
B	HOH920
D	HOH807
D	HOH808
D	HOH809

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	2
Details	ACT_SITE: ACT_SITE => ECO:0000269\|PubMed:15314233

Chain	Residue	Details
A	HIS144
B	HIS444

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000269\|PubMed:11701129, ECO:0000269\|PubMed:15314233, ECO:0000269\|PubMed:16916640

Chain	Residue	Details
A	CYS186
B	CYS486

site_id	SWS_FT_FI3
Number of Residues	6
Details	SITE: Cleavage; by CAPN1 => ECO:0000269\|PubMed:19617626

Chain	Residue	Details
A	PHE36
A	MET45
A	SER47
B	PHE336
B	MET345
B	SER347

site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Involved in allosteric regulation => ECO:0000269\|PubMed:15314233, ECO:0000269\|PubMed:19581639

Chain	Residue	Details
A	ARG187
A	TYR223
B	ARG487
B	TYR523

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N-acetylalanine => ECO:0007744\|PubMed:19413330, ECO:0007744\|PubMed:22223895

Chain	Residue	Details
A	ALA2
B	ALA302

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine; by PAK2 => ECO:0000269\|PubMed:21555521, ECO:0000269\|PubMed:27889207

Chain	Residue	Details
A	SER30
A	SER239
B	SER330
B	SER539

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER37
B	SER337

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by PAK2 => ECO:0000269\|PubMed:21555521, ECO:0000269\|PubMed:27889207

Chain	Residue	Details
A	THR173
B	THR473

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: (Microbial infection) ADP-riboxanated arginine => ECO:0000269\|PubMed:35338844, ECO:0000269\|PubMed:35446120

Chain	Residue	Details
A	ARG233
B	ARG533

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1qx3

Chain	Residue	Details
A	CYS186
A	GLY145
A	HIS144

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1qx3

Chain	Residue	Details
B	GLY445
B	HIS444
B	CYS486

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)