+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-33729 | |||||||||
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Title | Human propionyl-coenzyme A carboxylase | |||||||||
Map data | Human propionyl-coenzyme A carboxylase | |||||||||
Sample |
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Keywords | Cryo-EM / PCC / Mitochondria / CYTOSOLIC PROTEIN | |||||||||
Function / homology | Function and homology information short-chain fatty acid catabolic process / branched-chain amino acid metabolic process / Propionyl-CoA catabolism / propionyl-CoA carboxylase / propionyl-CoA carboxylase activity / Defective HLCS causes multiple carboxylase deficiency / Biotin transport and metabolism / biotin binding / catalytic complex / fatty acid metabolic process ...short-chain fatty acid catabolic process / branched-chain amino acid metabolic process / Propionyl-CoA catabolism / propionyl-CoA carboxylase / propionyl-CoA carboxylase activity / Defective HLCS causes multiple carboxylase deficiency / Biotin transport and metabolism / biotin binding / catalytic complex / fatty acid metabolic process / mitochondrial matrix / enzyme binding / mitochondrion / ATP binding / metal ion binding / cytosol Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) / human (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.2 Å | |||||||||
Authors | Su JY / Liu DS | |||||||||
Funding support | China, 1 items
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Citation | Journal: To Be Published Title: Human propionyl-coenzyme A carboxylase Authors: Su JY / Liu DS | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_33729.map.gz | 90.4 MB | EMDB map data format | |
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Header (meta data) | emd-33729-v30.xml emd-33729.xml | 14.7 KB 14.7 KB | Display Display | EMDB header |
Images | emd_33729.png | 142.2 KB | ||
Others | emd_33729_half_map_1.map.gz emd_33729_half_map_2.map.gz | 165 MB 165 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-33729 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-33729 | HTTPS FTP |
-Related structure data
Related structure data | 7ybuMC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_33729.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Annotation | Human propionyl-coenzyme A carboxylase | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.0825 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: Human propionyl-coenzyme A carboxylase half map A
File | emd_33729_half_map_1.map | ||||||||||||
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Annotation | Human propionyl-coenzyme A carboxylase half map A | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Human propionyl-coenzyme A carboxylase half map B
File | emd_33729_half_map_2.map | ||||||||||||
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Annotation | Human propionyl-coenzyme A carboxylase half map B | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Human propionyl-coenzyme A carboxylase heterododecomer
Entire | Name: Human propionyl-coenzyme A carboxylase heterododecomer |
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Components |
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-Supramolecule #1: Human propionyl-coenzyme A carboxylase heterododecomer
Supramolecule | Name: Human propionyl-coenzyme A carboxylase heterododecomer type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Propionyl-CoA carboxylase alpha chain, mitochondrial
Macromolecule | Name: Propionyl-CoA carboxylase alpha chain, mitochondrial / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO / EC number: propionyl-CoA carboxylase |
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Source (natural) | Organism: human (human) |
Molecular weight | Theoretical: 80.161922 KDa |
Sequence | String: MAGFWVGTAP LVAAGRRGRW PPQQLMLSAA LRTLKHVLYY SRQCLMVSRN LGSVGYDPNE KTFDKILVAN RGEIACRVIR TCKKMGIKT VAIHSDVDAS SVHVKMADEA VCVGPAPTSK SYLNMDAIME AIKKTRAQAV HPGYGFLSEN KEFARCLAAE D VVFIGPDT ...String: MAGFWVGTAP LVAAGRRGRW PPQQLMLSAA LRTLKHVLYY SRQCLMVSRN LGSVGYDPNE KTFDKILVAN RGEIACRVIR TCKKMGIKT VAIHSDVDAS SVHVKMADEA VCVGPAPTSK SYLNMDAIME AIKKTRAQAV HPGYGFLSEN KEFARCLAAE D VVFIGPDT HAIQAMGDKI ESKLLAKKAE VNTIPGFDGV VKDAEEAVRI AREIGYPVMI KASAGGGGKG MRIAWDDEET RD GFRLSSQ EAASSFGDDR LLIEKFIDNP RHIEIQVLGD KHGNALWLNE RECSIQRRNQ KVVEEAPSIF LDAETRRAMG EQA VALARA VKYSSAGTVE FLVDSKKNFY FLEMNTRLQV EHPVTECITG LDLVQEMIRV AKGYPLRHKQ ADIRINGWAV ECRV YAEDP YKSFGLPSIG RLSQYQEPLH LPGVRVDSGI QPGSDISIYY DPMISKLITY GSDRTEALKR MADALDNYVI RGVTH NIAL LREVIINSRF VKGDISTKFL SDVYPDGFKG HMLTKSEKNQ LLAIASSLFV AFQLRAQHFQ ENSRMPVIKP DIANWE LSV KLHDKVHTVV ASNNGSVFSV EVDGSKLNVT STWNLASPLL SVSVDGTQRT VQCLSREAGG NMSIQFLGTV YKVNILT RL AAELNKFMLE KVTEDTSSVL RSPMPGVVVA VSVKPGDAVA EGQEICVIEA MKMQNSMTAG KTGTVKSVHC QAGDTVGE G DLLVELE |
-Macromolecule #2: Propionyl-CoA carboxylase beta chain, mitochondrial
Macromolecule | Name: Propionyl-CoA carboxylase beta chain, mitochondrial / type: protein_or_peptide / ID: 2 / Number of copies: 6 / Enantiomer: LEVO / EC number: propionyl-CoA carboxylase |
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Source (natural) | Organism: human (human) |
Molecular weight | Theoretical: 58.284488 KDa |
Sequence | String: MAAALRVAAV GARLSVLASG LRAAVRSLCS QATSVNERIE NKRRTALLGG GQRRIDAQHK RGKLTARERI SLLLDPGSFV ESDMFVEHR CADFGMAADK NKFPGDSVVT GRGRINGRLV YVFSQDFTVF GGSLSGAHAQ KICKIMDQAI TVGAPVIGLN D SGGARIQE ...String: MAAALRVAAV GARLSVLASG LRAAVRSLCS QATSVNERIE NKRRTALLGG GQRRIDAQHK RGKLTARERI SLLLDPGSFV ESDMFVEHR CADFGMAADK NKFPGDSVVT GRGRINGRLV YVFSQDFTVF GGSLSGAHAQ KICKIMDQAI TVGAPVIGLN D SGGARIQE GVESLAGYAD IFLRNVTASG VIPQISLIMG PCAGGAVYSP ALTDFTFMVK DTSYLFITGP DVVKSVTNED VT QEELGGA KTHTTMSGVA HRAFENDVDA LCNLRDFFNY LPLSSQDPAP VRECHDPSDR LVPELDTIVP LESTKAYNMV DII HSVVDE REFFEIMPNY AKNIIVGFAR MNGRTVGIVG NQPKVASGCL DINSSVKGAR FVRFCDAFNI PLITFVDVPG FLPG TAQEY GGIIRHGAKL LYAFAEATVP KVTVITRKAY GGAYDVMSSK HLCGDTNYAW PTAEIAVMGA KGAVEIIFKG HENVE AAQA EYIEKFANPF PAAVRGFVDD IIQPSSTRAR ICCDLDVLAS KKVQRPWRKH ANIPL |
-Macromolecule #3: 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL
Macromolecule | Name: 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL type: ligand / ID: 3 / Number of copies: 6 / Formula: BTI |
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Molecular weight | Theoretical: 228.311 Da |
Chemical component information | ChemComp-BTI: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.3 µm |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: INSILICO MODEL |
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Initial angle assignment | Type: RANDOM ASSIGNMENT |
Final angle assignment | Type: COMMON LINE |
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 2.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 99377 |