6ROA | pdb_00006roa

Crystal structure of V57G mutant of human cystatin C

External Resource: Annotation

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d6roaa_	Alpha and beta proteins (a+b)	Cystatin-like	Cystatin/monellin	Cystatins	Cystatin C	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d6roab_	Alpha and beta proteins (a+b)	Cystatin-like	Cystatin/monellin	Cystatins	Cystatin C	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	Cystatin/monellin	8038736	3000441	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Cystatin/monellin	8038736	3000441	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	Cystatin	e6roaA1	A: a+b two layers	X: Cystatin-like	H: Cystatin/monellin (From Topology)	T: Cystatin/monellin	F: Cystatin	ECOD (1.6)
B	Cystatin	e6roaB1	A: a+b two layers	X: Cystatin-like	H: Cystatin/monellin (From Topology)	T: Cystatin/monellin	F: Cystatin	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.10.450.10	Alpha Beta	Roll	Nuclear Transport Factor 2	Chain: A,	CATH (utative)
B	3.10.450.10	Alpha Beta	Roll	Nuclear Transport Factor 2	Chain: A,	CATH (utative)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Cystatin-C	amide binding amyloid-beta binding binding peptide binding enzyme regulator activity molecular function inhibitor activity peptidase regulator activity molecular function regulator activity enzyme inhibitor activity cysteine-type endopeptidase inhibitor activity peptidase inhibitor activity endopeptidase regulator activity endopeptidase inhibitor activity protein binding amide binding amyloid-beta binding binding peptide binding enzyme regulator activity molecular function inhibitor activity peptidase regulator activity molecular function regulator activity enzyme inhibitor activity cysteine-type endopeptidase inhibitor activity peptidase inhibitor activity endopeptidase regulator activity endopeptidase inhibitor activity protein binding enzyme binding protease binding identical protein binding	developmental process multicellular organismal process negative regulation of tissue remodeling regulation of biological process regulation of developmental process negative regulation of developmental process negative regulation of biological process biological regulation regulation of tissue remodeling regulation of blood vessel remodeling anatomical structure morphogenesis blood vessel remodeling negative regulation of blood vessel remodeling tissue remodeling anatomical structure development developmental process multicellular organismal process negative regulation of tissue remodeling regulation of biological process regulation of developmental process negative regulation of developmental process negative regulation of biological process biological regulation regulation of tissue remodeling regulation of blood vessel remodeling anatomical structure morphogenesis blood vessel remodeling negative regulation of blood vessel remodeling tissue remodeling anatomical structure development regulation of multicellular organismal process negative regulation of multicellular organismal process regulation of anatomical structure morphogenesis negative regulation of proteolysis regulation of cellular process regulation of protein metabolic process negative regulation of metabolic process primary metabolic process regulation of macromolecule metabolic process regulation of primary metabolic process regulation of proteolysis proteolysis negative regulation of cellular process metabolic process cellular process protein metabolic process macromolecule metabolic process regulation of metabolic process negative regulation of protein metabolic process negative regulation of macromolecule metabolic process negative regulation of catabolic process negative regulation of collagen metabolic process catabolic process negative regulation of collagen catabolic process regulation of catabolic process regulation of collagen metabolic process collagen catabolic process regulation of collagen catabolic process collagen metabolic process response to stimulus defense response response to stress negative regulation of hydrolase activity regulation of catalytic activity negative regulation of catalytic activity negative regulation of peptidase activity negative regulation of molecular function regulation of peptidase activity regulation of molecular function regulation of hydrolase activity carbohydrate derivative metabolic process macromolecule catabolic process negative regulation of protein catabolic process negative regulation of elastin catabolic process negative regulation of glycoprotein metabolic process carbohydrate derivative catabolic process glycoprotein catabolic process elastin catabolic process regulation of elastin catabolic process protein catabolic process glycoprotein metabolic process elastin metabolic process regulation of glycoprotein metabolic process regulation of protein catabolic process cellular component disassembly negative regulation of extracellular matrix organization extracellular matrix disassembly regulation of cellular component organization negative regulation of cellular component organization extracellular matrix organization cellular component organization negative regulation of extracellular matrix disassembly cellular component organization or biogenesis regulation of extracellular matrix organization regulation of extracellular matrix disassembly extracellular structure organization external encapsulating structure organization supramolecular fiber organization	membrane-bounded organelle cellular anatomical structure organelle vesicle extracellular exosome extracellular vesicle extracellular organelle extracellular region extracellular space extracellular membrane-bounded organelle cell periphery plasma membrane membrane intracellular anatomical structure membrane-bounded organelle cellular anatomical structure organelle vesicle extracellular exosome extracellular vesicle extracellular organelle extracellular region extracellular space extracellular membrane-bounded organelle cell periphery plasma membrane membrane intracellular anatomical structure cytoplasm membrane-enclosed lumen intracellular vesicle ficolin-1-rich granule intracellular membrane-bounded organelle endomembrane system intracellular organelle lumen intracellular organelle organelle lumen cytoplasmic vesicle ficolin-1-rich granule lumen secretory granule secretory vesicle tertiary granule lumen tertiary granule Golgi apparatus endoplasmic reticulum lumen endoplasmic reticulum

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR000010	Cystatin domain	Domain
A, B	IPR046350	Cystatin superfamily	Homologous Superfamily
A, B	IPR018073	Proteinase inhibitor I25, cystatin, conserved site	Conserved Site

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: P01034	ACys amyloidosis age related macular degeneration 11 Alzheimer disease acute myeloid leukemia meningioma oral submucous fibrosis secretory meningioma amyotrophic lateral sclerosis type 1 angiomatous meningioma intraorbital meningioma benign meningioma cerebral convexity meningioma meningothelial meningioma olfactory groove meningioma fibrous meningioma ACys amyloidosis age related macular degeneration 11 Alzheimer disease acute myeloid leukemia meningioma oral submucous fibrosis secretory meningioma amyotrophic lateral sclerosis type 1 angiomatous meningioma intraorbital meningioma benign meningioma cerebral convexity meningioma meningothelial meningioma olfactory groove meningioma fibrous meningioma parasagittal meningioma amyloidosis intraventricular meningioma spinal meningioma cardiovascular disease clear cell meningioma microcystic meningioma age-related macular degeneration psammomatous meningioma kidney disease transitional meningioma poisoning primitive neuroectodermal tumor hypertensive disorder Recurrence kidney failure tuberculosis cerebral amyloid angiopathy, APP-related lymphoplasmacyte-rich meningioma malignant glioma ABri amyloidosis medulloblastoma acute kidney failure diabetes mellitus Down syndrome exocrine pancreatic carcinoma ovarian cancer gastric carcinoma proteinuria inborn carbohydrate metabolic disorder retinal degeneration atypical teratoid rhabdoid tumor macular degeneration acquired metabolic disease ADan amyloidosis pancreatic intraductal papillary-mucinous neoplasm Finnish type amyloidosis periodic fever syndrome glioblastoma B-cell chronic lymphocytic leukemia cerebral amyloid angiopathy large cell medulloblastoma malignant ependymoma malignant pancreatic neoplasm coronary artery disease non-small cell lung carcinoma osteosarcoma papillary meningioma gastric cancer

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.