4JJ8

Caspase-3 specific unnatural amino acid peptides

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations
Protein Modification Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4jj8a_	Alpha and beta proteins (a/b)	Caspase-like	Caspase-like	Caspase catalytic domain	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d4jj8b_	Alpha and beta proteins (a/b)	Caspase-like	Caspase-like	Caspase catalytic domain	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Caspase-like	8033647	3001096	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Caspase-like	8033647	3001096	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Peptidase_C14	e4jj8A2	A: a/b three-layered sandwiches	X: Caspase-like (From Topology)	H: Caspase-like (From Topology)	T: Caspase-like	F: Peptidase_C14	ECOD (1.6)
B	Peptidase_C14	e4jj8B2	A: a/b three-layered sandwiches	X: Caspase-like (From Topology)	H: Caspase-like (From Topology)	T: Caspase-like	F: Peptidase_C14	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1460	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
B	3.40.50.1460	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00656	Caspase domain (Peptidase_C14)	Caspase domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
C, D	Caspase Inhibitor	-	-	-
A, B	Caspase-7	peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity cysteine-type peptidase activity cysteine-type endopeptidase activity endopeptidase activity RNA binding binding organic cyclic compound binding nucleic acid binding aspartic-type peptidase activity aspartic-type endopeptidase activity	developmental process heart development multicellular organism development multicellular organismal process anatomical structure development animal organ development circulatory system development system development cellular process apoptotic process cell death programmed cell death catabolic process metabolic process developmental process heart development multicellular organism development multicellular organismal process anatomical structure development animal organ development circulatory system development system development cellular process apoptotic process cell death programmed cell death catabolic process metabolic process primary metabolic process protein catabolic process protein metabolic process macromolecule metabolic process macromolecule catabolic process regulation of biological process neuron apoptotic process positive regulation of programmed cell death regulation of cellular process regulation of apoptotic process biological regulation positive regulation of biological process regulation of programmed cell death positive regulation of apoptotic process positive regulation of neuron apoptotic process positive regulation of cellular process regulation of neuron apoptotic process cellular response to stimulus biological process involved in interspecies interaction between organisms response to lipid response to stimulus response to other organism cellular response to lipopolysaccharide response to oxygen-containing compound response to external stimulus cellular response to molecule of bacterial origin response to lipopolysaccharide cellular response to oxygen-containing compound response to biotic stimulus cellular response to biotic stimulus cellular response to chemical stimulus response to chemical response to bacterium cellular response to lipid response to external biotic stimulus response to molecule of bacterial origin lymphocyte apoptotic process leukocyte apoptotic process execution phase of apoptosis gene expression macromolecule biosynthetic process protein maturation biosynthetic process proteolysis protein processing defense response defense response to bacterium defense response to other organism response to stress fibroblast apoptotic process cellular response to nitrogen compound cellular response to staurosporine cellular response to organic cyclic compound response to staurosporine response to nitrogen compound response to alkaloid cellular response to alkaloid response to organic cyclic compound membrane organization wound healing regulation of cellular component organization positive regulation of cellular component organization plasma membrane repair cellular component organization regulation of plasma membrane organization plasma membrane organization regulation of plasma membrane repair cellular component organization or biogenesis positive regulation of plasma membrane repair response to wounding endomembrane system organization response to light stimulus response to radiation response to abiotic stimulus response to UV muscle structure development cellular developmental process cell differentiation striated muscle cell differentiation muscle cell differentiation	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen organelle nuclear lumen cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen organelle nuclear lumen extracellular region extracellular space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR001309	Peptidase C14, p20 domain	Domain
A, B	IPR011600	Peptidase C14, caspase domain	Domain
A, B	IPR016129	Peptidase family C14A, His active site	Active Site
A, B	IPR015917	Peptidase C14A, caspase catalytic domain	Domain
A, B	IPR029030	Caspase-like domain superfamily	Homologous Superfamily
A, B	IPR033139	Peptidase family C14A, cysteine active site	Active Site
A, B	IPR002138	Peptidase C14, caspase non-catalytic subunit p10	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: P55210	vitiligo acute myeloid leukemia breast carcinoma Myocardial Reperfusion Injury pancreatic intraductal papillary-mucinous carcinoma attention deficit hyperactivity disorder, inattentive type juvenile dermatomyositis lung carcinoma medulloblastoma pancreatic intraductal papillary-mucinous neoplasm Barrett esophagus cancer large cell medulloblastoma malignant colon neoplasm psoriasis vitiligo acute myeloid leukemia breast carcinoma Myocardial Reperfusion Injury pancreatic intraductal papillary-mucinous carcinoma attention deficit hyperactivity disorder, inattentive type juvenile dermatomyositis lung carcinoma medulloblastoma pancreatic intraductal papillary-mucinous neoplasm Barrett esophagus cancer large cell medulloblastoma malignant colon neoplasm psoriasis breast cancer esophageal adenocarcinoma malignant glioma

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
C, D	1MH
C, D	1U8
C, D	ACE	RESID: AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354 PSI-MOD : N-acetyl-L-alanine MOD:00050 , N-acetyl-L-aspartic acid MOD:00051 , N-acetyl-L-cysteine MOD:00052 , N-acetyl-S-archeol-cysteine MOD:00897 , N-acetyl-L-glutamic acid MOD:00053 , N-acetyl-L-glutamine MOD:00054 , N-acetylglycine MOD:00055 , N-acetyl-L-methionine MOD:00058 , N-acetyl-L-proline MOD:00059 , N-acetyl-L-serine MOD:00060 , N,O-diacetylated L-serine MOD:00648 , N-acetyl-L-threonine MOD:00061 , N-acetyl-L-tyrosine MOD:00062 , N-acetyl-L-valine MOD:00063 , N2-acetyl-L-arginine MOD:00359
C, D	B3L	RESID: AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354
C, D	HLX	RESID: AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.