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- EMDB-36706: Human 3-methylcrotonyl-CoA carboxylase in BCCP-H1 state with MCoA -
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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Human 3-methylcrotonyl-CoA carboxylase in BCCP-H1 state with MCoA | |||||||||
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![]() | MCC / Mitochondrial / CYTOSOLIC PROTEIN | |||||||||
Function / homology | ![]() 3-methylcrotonyl-CoA carboxylase complex, mitochondrial / methylcrotonoyl-CoA carboxylase / biotin metabolic process / methylcrotonoyl-CoA carboxylase complex / urea carboxylase activity / Defective HLCS causes multiple carboxylase deficiency / methylcrotonoyl-CoA carboxylase activity / Biotin transport and metabolism / propionyl-CoA carboxylase activity / L-leucine catabolic process ...3-methylcrotonyl-CoA carboxylase complex, mitochondrial / methylcrotonoyl-CoA carboxylase / biotin metabolic process / methylcrotonoyl-CoA carboxylase complex / urea carboxylase activity / Defective HLCS causes multiple carboxylase deficiency / methylcrotonoyl-CoA carboxylase activity / Biotin transport and metabolism / propionyl-CoA carboxylase activity / L-leucine catabolic process / biotin carboxylase activity / branched-chain amino acid catabolic process / Branched-chain amino acid catabolism / coenzyme A metabolic process / biotin binding / mitochondrial matrix / mitochondrion / ATP binding / metal ion binding / cytosol Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||
![]() | Liu DS / Su JY / Tian XY | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Human 3-methylcrotonyl-CoA carboxylase in BCCP-H1 state with substrate Authors: Liu DS / Su JY | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 89.4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 15.3 KB 15.3 KB | Display Display | ![]() |
Images | ![]() | 121.9 KB | ||
Filedesc metadata | ![]() | 6.1 KB | ||
Others | ![]() ![]() | 165.1 MB 165.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.2 MB | Display | ![]() |
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Full document | ![]() | 1.2 MB | Display | |
Data in XML | ![]() | 15 KB | Display | |
Data in CIF | ![]() | 17.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8jxnMC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||
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Voxel size | X=Y=Z: 0.97 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_36706_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_36706_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Dodecamer of human MCC
Entire | Name: Dodecamer of human MCC |
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Components |
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-Supramolecule #1: Dodecamer of human MCC
Supramolecule | Name: Dodecamer of human MCC / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
Macromolecule | Name: Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO / EC number: methylcrotonoyl-CoA carboxylase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 61.406027 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MWAVLRLALR PCARASPAGP RAYHGDSVAS LGTQPDLGSA LYQENYKQMK ALVNQLHERV EHIKLGGGEK ARALHISRGK LLPRERIDN LIDPGSPFLE LSQFAGYQLY DNEEVPGGGI ITGIGRVSGV ECMIIANDAT VKGGAYYPVT VKKQLRAQEI A MQNRLPCI ...String: MWAVLRLALR PCARASPAGP RAYHGDSVAS LGTQPDLGSA LYQENYKQMK ALVNQLHERV EHIKLGGGEK ARALHISRGK LLPRERIDN LIDPGSPFLE LSQFAGYQLY DNEEVPGGGI ITGIGRVSGV ECMIIANDAT VKGGAYYPVT VKKQLRAQEI A MQNRLPCI YLVDSGGAYL PRQADVFPDR DHFGRTFYNQ AIMSSKNIAQ IAVVMGSCTA GGAYVPAMAD ENIIVRKQGT IF LAGPPLV KAATGEEVSA EDLGGADLHC RKSGVSDHWA LDDHHALHLT RKVVRNLNYQ KKLDVTIEPS EEPLFPADEL YGI VGANLK RSFDVREVIA RIVDGSRFTE FKAFYGDTLV TGFARIFGYP VGIVGNNGVL FSESAKKGTH FVQLCCQRNI PLLF LQNIT GFMVGREYEA EGIAKDGAKM VAAVACAQVP KITLIIGGSY GAGNYGMCGR AYSPRFLYIW PNARISVMGG EQAAN VLAT ITKDQRAREG KQFSSADEAA LKEPIIKKFE EEGNPYYSSA RVWDDGIIDP ADTRLVLGLS FSAALNAPIE KTDFGI FRM UniProtKB: Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial |
-Macromolecule #2: Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
Macromolecule | Name: Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial type: protein_or_peptide / ID: 2 / Number of copies: 6 / Enantiomer: LEVO / EC number: methylcrotonoyl-CoA carboxylase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 80.584016 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MAAASAVSVL LVAAERNRWH RLPSLLLPPR TWVWRQRTMK YTTATGRNIT KVLIANRGEI ACRVMRTAKK LGVQTVAVYS EADRNSMHV DMADEAYSIG PAPSQQSYLS MEKIIQVAKT SAAQAIHPGC GFLSENMEFA ELCKQEGIIF IGPPPSAIRD M GIKSTSKS ...String: MAAASAVSVL LVAAERNRWH RLPSLLLPPR TWVWRQRTMK YTTATGRNIT KVLIANRGEI ACRVMRTAKK LGVQTVAVYS EADRNSMHV DMADEAYSIG PAPSQQSYLS MEKIIQVAKT SAAQAIHPGC GFLSENMEFA ELCKQEGIIF IGPPPSAIRD M GIKSTSKS IMAAAGVPVV EGYHGEDQSD QCLKEHARRI GYPVMIKAVR GGGGKGMRIV RSEQEFQEQL ESARREAKKS FN DDAMLIE KFVDTPRHVE VQVFGDHHGN AVYLFERDCS VQRRHQKIIE EAPAPGIKSE VRKKLGEAAV RAAKAVNYVG AGT VEFIMD SKHNFCFMEM NTRLQVEHPV TEMITGTDLV EWQLRIAAGE KIPLSQEEIT LQGHAFEARI YAEDPSNNFM PVAG PLVHL STPRADPSTR IETGVRQGDE VSVHYDPMIA KLVVWAADRQ AALTKLRYSL RQYNIVGLHT NIDFLLNLSG HPEFE AGNV HTDFIPQHHK QLLLSRKAAA KESLCQAALG LILKEKAMTD TFTLQAHDQF SPFSSSSGRR LNISYTRNMT LKDGKN NVA IAVTYNHDGS YSMQIEDKTF QVLGNLYSEG DCTYLKCSVN GVASKAKLII LENTIYLFSK EGSIEIDIPV PKYLSSV SS QETQGGPLAP MTGTIEKVFV KAGDKVKAGD SLMVMIAMKM EHTIKSPKDG TVKKVFYREG AQANRHTPLV EFEEEESD K RESE UniProtKB: Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial |
-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: |
-Macromolecule #4: ~{S}-[2-[3-[[(2~{R})-4-[[[(2~{S},3~{S},4~{S},5~{S})-5-(6-aminopur...
Macromolecule | Name: ~{S}-[2-[3-[[(2~{R})-4-[[[(2~{S},3~{S},4~{S},5~{S})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl- ...Name: ~{S}-[2-[3-[[(2~{R})-4-[[[(2~{S},3~{S},4~{S},5~{S})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethyl] 3-methylbut-2-enethioate type: ligand / ID: 4 / Number of copies: 6 / Formula: TW3 |
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Molecular weight | Theoretical: 849.635 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.5 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: INSILICO MODEL |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 43147 |
Initial angle assignment | Type: RANDOM ASSIGNMENT |
Final angle assignment | Type: ANGULAR RECONSTITUTION |