3O5Q

Fk1 domain mutant A19T of FKBP51, crystal form IV, in presence of DMSO

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3o5qa1	Alpha and beta proteins (a+b)	FKBP-like	FKBP-like	FKBP immunophilin/proline isomerase	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d3o5qa2	Artifacts	Tags	Tags	Tags	N-terminal Tags	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	Rotamase-like	8042824	3000622	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	FKBP_C	e3o5qA1	A: a+b two layers	X: FKBP-like	H: FKBP-like	T: FKBP-like	F: FKBP_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.10.50.40	Alpha Beta	Roll	Chitinase A	domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00254	FKBP-type peptidyl-prolyl cis-trans isomerase (FKBP_C)	FKBP-type peptidyl-prolyl cis-trans isomerase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Peptidyl-prolyl cis-trans isomerase FKBP5	isomerase activity catalytic activity, acting on a protein peptidyl-prolyl cis-trans isomerase activity catalytic activity cis-trans isomerase activity FK506 binding amide binding binding organic cyclic compound binding macrolide binding protein binding heat shock protein binding protein-macromolecule adaptor activity molecular adaptor activity	cellular biosynthetic process cellular metabolic process primary metabolic process gene expression macromolecule biosynthetic process protein maturation protein folding biosynthetic process metabolic process cellular process protein metabolic process macromolecule metabolic process biological process involved in interspecies interaction between organisms response to stimulus cellular biosynthetic process cellular metabolic process primary metabolic process gene expression macromolecule biosynthetic process protein maturation protein folding biosynthetic process metabolic process cellular process protein metabolic process macromolecule metabolic process biological process involved in interspecies interaction between organisms response to stimulus response to other organism response to bacterium response to external stimulus response to external biotic stimulus response to biotic stimulus chaperone-mediated protein folding	membrane cellular anatomical entity extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol membrane cellular anatomical entity extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen nuclear lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR046357	Peptidyl-prolyl cis-trans isomerase domain superfamily	Homologous Superfamily
A	IPR050754	Peptidyl-prolyl cis-trans isomerase FKBP4/5/8-like	Family
A	IPR011990	Tetratricopeptide-like helical domain superfamily	Homologous Superfamily
A	IPR001179	FKBP-type peptidyl-prolyl cis-trans isomerase domain	Domain
A	IPR019734	Tetratricopeptide repeat	Repeat

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: Q13451	rheumatoid arthritis endometriosis major depressive disorder Neurobehavioral Manifestations glioblastoma ovarian cancer hepatocellular carcinoma pancreatic intraductal papillary-mucinous neoplasm pilocytic astrocytoma astrocytic tumor lung lymphangioleiomyomatosis bipolar disorder Sjogren syndrome colorectal cancer malignant glioma rheumatoid arthritis endometriosis major depressive disorder Neurobehavioral Manifestations glioblastoma ovarian cancer hepatocellular carcinoma pancreatic intraductal papillary-mucinous neoplasm pilocytic astrocytoma astrocytic tumor lung lymphangioleiomyomatosis bipolar disorder Sjogren syndrome colorectal cancer malignant glioma tuberous sclerosis disappearing bone disease myopathy gastric cancer Hashimoto thyroiditis pancreatic ductal adenocarcinoma hydrolethalus syndrome pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia interstitial cystitis anxiety disorder lung adenocarcinoma atopic eczema cystic fibrosis malignant pancreatic neoplasm Duchenne muscular dystrophy mood disorder gastric carcinoma opiate dependence heart disease pancreatic intraductal papillary-mucinous carcinoma hypothyroidism Pick disease large cell medulloblastoma psoriasis asthma lung cancer renal cell carcinoma atypical teratoid rhabdoid tumor lymphangioma sinusitis colorectal adenoma malignant ependymoma tuberculosis depressive disorder medulloblastoma Emery-Dreifuss muscular dystrophy exocrine pancreatic carcinoma

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.