Entry Database : PDB / ID : 2bit Structure visualization Downloads & linksTitle Crystal structure of human cyclophilin D at 1.7 A resolution ComponentsPEPTIDYL-PROLYL CIS-TRANS ISOMERASE Details Keywords ISOMERASE / CRYSTAL ENGINEERING / CIS-TRAN-ISOMERIZATION / HUMAN / MITOCHONDRIAL PROTEINFunction / homology Function and homology informationFunction Domain/homology Component
regulation of proton-transporting ATPase activity, rotational mechanism / negative regulation of oxidative phosphorylation uncoupler activity / mitochondrial outer membrane permeabilization involved in programmed cell death / regulation of mitochondrial membrane permeability involved in programmed necrotic cell death / skeletal muscle fiber differentiation / mitochondrial permeability transition pore complex / mitochondrial depolarization / cellular response to arsenic-containing substance / negative regulation of ATP-dependent activity / negative regulation of oxidative phosphorylation ... regulation of proton-transporting ATPase activity, rotational mechanism / negative regulation of oxidative phosphorylation uncoupler activity / mitochondrial outer membrane permeabilization involved in programmed cell death / regulation of mitochondrial membrane permeability involved in programmed necrotic cell death / skeletal muscle fiber differentiation / mitochondrial permeability transition pore complex / mitochondrial depolarization / cellular response to arsenic-containing substance / negative regulation of ATP-dependent activity / negative regulation of oxidative phosphorylation / regulation of mitochondrial membrane permeability / cyclosporin A binding / negative regulation of release of cytochrome c from mitochondria / apoptotic mitochondrial changes / necroptotic process / protein peptidyl-prolyl isomerization / negative regulation of intrinsic apoptotic signaling pathway / cellular response to calcium ion / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / response to ischemia / cellular response to hydrogen peroxide / protein folding / mitochondrial inner membrane / mitochondrial matrix / negative regulation of apoptotic process / mitochondrion / membrane / cytoplasm Similarity search - Function Cyclophilin-like / Cyclophilin / Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved site / Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. / Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain profile. / Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain / Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD / Cyclophilin-like domain superfamily / Beta Barrel / Mainly Beta Similarity search - Domain/homologyBiological species HOMO SAPIENS (human)Method X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution : 1.71 Å DetailsAuthors Hennig, M. / Thoma, R. / Stihle, M. / Schlatter, D. CitationJournal : Acta Crystallogr.,Sect.D / Year : 2005Title : Crystal Engineering Yields Crystals of Cyclophilin D Diffracting to 1.7 A ResolutionAuthors : Schlatter, D. / Thoma, R. / Kueng, E. / Stihle, M. / Mueller, F. / Boroni, E. / Hennig, M. History Deposition Jan 26, 2005 Deposition site : PDBE / Processing site : PDBERevision 1.0 Jan 26, 2005 Provider : repository / Type : Initial releaseRevision 1.1 May 8, 2011 Group : Version format complianceRevision 1.2 Jul 13, 2011 Group : Version format complianceRevision 1.3 Jun 13, 2018 Group : Data collection / Database references / Category : citation / Item : _citation.page_lastRevision 1.4 Dec 13, 2023 Group : Data collection / Database references ... Data collection / Database references / Other / Refinement description Category : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf
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