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- PDB-4bej: Nucleotide-free Dynamin 1-like protein (DNM1L, DRP1, DLP1) -

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Basic information

Entry
Database: PDB / ID: 4bej
TitleNucleotide-free Dynamin 1-like protein (DNM1L, DRP1, DLP1)
ComponentsDYNAMIN 1-LIKE PROTEIN
KeywordsHYDROLASE / G PROTEIN / MITOCHONDRIAL FISSION / MEMBRANE REMODELING / APOPTOSIS
Function / homology
Function and homology information


mitochondrial membrane fission / regulation of ATP metabolic process / regulation of peroxisome organization / mitocytosis / regulation of mitophagy / dynamin GTPase / Apoptotic execution phase / peroxisome fission / mitochondrial fragmentation involved in apoptotic process / GTP-dependent protein binding ...mitochondrial membrane fission / regulation of ATP metabolic process / regulation of peroxisome organization / mitocytosis / regulation of mitophagy / dynamin GTPase / Apoptotic execution phase / peroxisome fission / mitochondrial fragmentation involved in apoptotic process / GTP-dependent protein binding / protein localization to mitochondrion / mitochondrial fission / positive regulation of neutrophil chemotaxis / regulation of mitochondrion organization / positive regulation of mitochondrial fission / intracellular distribution of mitochondria / heart contraction / necroptotic process / positive regulation of release of cytochrome c from mitochondria / brush border / localization / positive regulation of intrinsic apoptotic signaling pathway / clathrin-coated pit / mitochondrion organization / GTPase activator activity / release of cytochrome c from mitochondria / positive regulation of protein secretion / synaptic vesicle membrane / small GTPase binding / peroxisome / endocytosis / rhythmic process / calcium ion transport / protein complex oligomerization / microtubule binding / regulation of gene expression / protein-containing complex assembly / microtubule / mitochondrial outer membrane / membrane fusion / molecular adaptor activity / positive regulation of apoptotic process / intracellular membrane-bounded organelle / GTPase activity / lipid binding / ubiquitin protein ligase binding / GTP binding / endoplasmic reticulum membrane / perinuclear region of cytoplasm / Golgi apparatus / endoplasmic reticulum / protein homodimerization activity / protein-containing complex / mitochondrion / membrane / identical protein binding / cytosol / cytoplasm
Similarity search - Function
Dynamin, middle domain / Dynamin GTPase effector / Dynamin GTPase effector domain / Dynamin GTPase effector domain / Dynamin, GTPase region, conserved site / Dynamin-type guanine nucleotide-binding (G) domain signature. / Dynamin stalk domain / Dynamin central region / GTPase effector domain / GED domain profile. ...Dynamin, middle domain / Dynamin GTPase effector / Dynamin GTPase effector domain / Dynamin GTPase effector domain / Dynamin, GTPase region, conserved site / Dynamin-type guanine nucleotide-binding (G) domain signature. / Dynamin stalk domain / Dynamin central region / GTPase effector domain / GED domain profile. / Dynamin, GTPase domain / Dynamin, GTPase / Dynamin / Dynamin-type guanine nucleotide-binding (G) domain / Dynamin-type guanine nucleotide-binding (G) domain profile. / Dynamin, N-terminal / Dynamin family / Four Helix Bundle (Hemerythrin (Met), subunit A) / P-loop containing nucleotide triphosphate hydrolases / Up-down Bundle / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Dynamin-1-like protein
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.483 Å
AuthorsFroehlich, C. / Schwefel, D. / Faelber, K. / Daumke, O.
CitationJournal: Embo J. / Year: 2013
Title: Structural Insights Into Oligomerization and Mitochondrial Remodelling of Dynamin 1-Like Protein.
Authors: Frohlich, C. / Grabiger, S. / Schwefel, D. / Faelber, K. / Rosenbaum, E. / Mears, J. / Rocks, O. / Daumke, O.
History
DepositionMar 11, 2013Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 24, 2013Provider: repository / Type: Initial release
Revision 1.1May 22, 2013Group: Database references
Revision 1.2Dec 20, 2023Group: 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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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: DYNAMIN 1-LIKE PROTEIN
B: DYNAMIN 1-LIKE PROTEIN
C: DYNAMIN 1-LIKE PROTEIN
D: DYNAMIN 1-LIKE PROTEIN


Theoretical massNumber of molelcules
Total (without water)276,8424
Polymers276,8424
Non-polymers00
Water0
1
A: DYNAMIN 1-LIKE PROTEIN
B: DYNAMIN 1-LIKE PROTEIN


Theoretical massNumber of molelcules
Total (without water)138,4212
Polymers138,4212
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2310 Å2
ΔGint-13.8 kcal/mol
Surface area54650 Å2
MethodPISA
2
C: DYNAMIN 1-LIKE PROTEIN
D: DYNAMIN 1-LIKE PROTEIN


Theoretical massNumber of molelcules
Total (without water)138,4212
Polymers138,4212
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2210 Å2
ΔGint-14.4 kcal/mol
Surface area54350 Å2
MethodPISA
Unit cell
Length a, b, c (Å)101.470, 80.770, 208.272
Angle α, β, γ (deg.)90.00, 93.45, 90.00
Int Tables number3
Space group name H-MP121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
22
33
44
55
/ NCS ensembles :
ID
1
2
3
4
5

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Components

#1: Protein
DYNAMIN 1-LIKE PROTEIN / DNM1P/VPS1P-LIKE PROTEIN / DVLP / DYNAMIN FAMILY MEMBER PROLINE-RICH CARBOXYL-TERMINAL DOMAIN LESS ...DNM1P/VPS1P-LIKE PROTEIN / DVLP / DYNAMIN FAMILY MEMBER PROLINE-RICH CARBOXYL-TERMINAL DOMAIN LESS / DYMPLE / DYNAMIN-LIKE PROTEIN / DYNAMIN-LIKE PROTEIN 4 / DYNAMIN-LIKE PROTEIN IV / HDYNIV / DYNAMIN-RELATED PROTEIN 1


Mass: 69210.516 Da / Num. of mol.: 4 / Fragment: DNM1L DELTA B INSERT, RESIDUES 1-516,632-725 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: MODIFIED PET28A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA / References: UniProt: O00429, dynamin GTPase
Sequence detailsHUMAN DNM1L ISOFORM 2

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.66 Å3/Da / Density % sol: 53.83 % / Description: NONE
Crystal growpH: 7.5 / Details: 12% PEG3350, 50 MM K(HCOO), pH 7.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: BESSY / Beamline: 14.1 / Wavelength: 0.91841
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Nov 24, 2010 / Details: MIRRORS
RadiationMonochromator: SI111 DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.91841 Å / Relative weight: 1
ReflectionResolution: 3.48→50 Å / Num. obs: 42403 / % possible obs: 97.3 % / Observed criterion σ(I): -3 / Redundancy: 3.94 % / Biso Wilson estimate: 75.8 Å2 / Rmerge(I) obs: 0.21 / Net I/σ(I): 10.19
Reflection shellResolution: 3.48→3.69 Å / Redundancy: 3.68 % / Rmerge(I) obs: 0.68 / Mean I/σ(I) obs: 2.41 / % possible all: 84.3

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Processing

Software
NameClassification
Cootmodel building
XDSdata scaling
XDSphasing
CCP4phasing
PHENIXphasing
Cootphasing
PHENIXrefinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3SNH
Resolution: 3.483→47.574 Å / SU ML: 0.48 / σ(F): 1.99 / Phase error: 28.78 / Stereochemistry target values: ML / Details: TORSION NCS USED.
RfactorNum. reflection% reflection
Rfree0.2761 2121 5 %
Rwork0.2509 --
obs0.2522 42384 97.27 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.483→47.574 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17076 0 0 0 17076
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00717286
X-RAY DIFFRACTIONf_angle_d1.61823356
X-RAY DIFFRACTIONf_dihedral_angle_d15.0486596
X-RAY DIFFRACTIONf_chiral_restr0.0812844
X-RAY DIFFRACTIONf_plane_restr0.0062960
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.483-3.5640.3583860.33641674X-RAY DIFFRACTION62
3.564-3.65310.35441370.31832760X-RAY DIFFRACTION100
3.6531-3.75180.32221480.31252708X-RAY DIFFRACTION100
3.7518-3.86220.35611380.29812758X-RAY DIFFRACTION100
3.8622-3.98680.29321380.29072741X-RAY DIFFRACTION100
3.9868-4.12920.27531550.27142705X-RAY DIFFRACTION100
4.1292-4.29440.29121580.24092736X-RAY DIFFRACTION100
4.2944-4.48970.28481370.23542756X-RAY DIFFRACTION100
4.4897-4.72620.24781520.22452746X-RAY DIFFRACTION100
4.7262-5.02210.28681230.22662780X-RAY DIFFRACTION100
5.0221-5.40930.26351450.24582759X-RAY DIFFRACTION100
5.4093-5.95270.27321490.26772765X-RAY DIFFRACTION100
5.9527-6.8120.32011400.27552782X-RAY DIFFRACTION100
6.812-8.57420.23321410.22392792X-RAY DIFFRACTION100
8.5742-47.57810.22591740.20152801X-RAY DIFFRACTION98
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
17.7148-1.6877-4.79457.88731.28452.9884-0.2047-0.5287-0.37260.05290.21870.10020.45260.50590.14270.39370.2777-0.00510.6018-0.05750.2225-41.908912.253718.2084
24.7462-0.9294-4.16726.18042.59679.5058-0.24440.2199-0.233-0.37670.00960.61170.47280.11890.11070.81060.0573-0.07420.6324-0.40860.81228.3859-41.9242-103.3135
31.96650.93731.87113.61061.67523.15330.19350.2274-0.2459-0.17450.0977-0.12370.38770.5464-0.44590.47940.1391-0.30430.9223-0.59180.8656-19.7389-11.328119.8418
48.38220.7178-3.07417.8424-0.29117.2346-0.0406-0.59620.48620.33150.19810.0184-0.05220.4113-0.09030.1513-0.02690.09250.5934-0.1710.456942.2793-103.1032-81.1217
52.2332-0.6754-0.22971.95840.01442.30290.0450.0560.31990.2681-0.0324-0.0242-0.58650.1263-0.12220.43350.30130.11710.4854-0.15590.3215-40.540828.503827.524
61.52960.95740.14382.22840.29811.9281-0.091-0.299-0.1295-0.0438-0.54830.21060.4466-0.5685-0.47620.4752-0.1378-0.10490.4958-0.52650.435734.955-59.1446-107.7838
71.83390.1942-0.0942.41610.3062.24640.25240.5023-0.4478-0.1351-0.1235-0.38430.14770.6978-0.10730.2370.08-0.03210.676-0.19030.4684-7.49112.192625.0025
81.56980.3017-0.25751.20230.18482.2455-0.2625-0.4166-0.02920.7855-0.1063-0.64680.57760.1031-0.8850.6559-0.1452-0.35180.3269-0.3740.508750.6379-119.0988-74.4966
92.0357-0.4204-0.11441.8775-0.00561.74850.0114-0.3590.2115-0.06640.07430.2425-0.0594-0.14410.0115-0.0867-0.1734-0.0440.0155-0.00360.0641-24.6927-4.8882-45.9827
102.04830.50010.29912.86940.57422.0983-0.00750.3936-0.2118-0.28820.0834-0.14020.37090.36480.12860.2517-0.0696-0.02040.0280.00490.1101-17.1603-24.0885-57.2461
112.5242-0.82660.10912.58170.11682.40480.0193-0.23440.4293-0.13280.0143-0.1659-0.7281-0.06-0.02240.1958-0.064-0.02540.0318-0.09570.2097-17.3261-43.8467-43.7575
122.67460.18430.39932.42090.18781.9370.06620.1402-0.58240.0212-0.0817-0.14550.16370.15320.0870.0866-0.08650.0651-0.0515-0.09220.2894-12.9525-66.4275-51.816
131.67980.1293-0.23945.12511.41236.8993-0.00550.4436-0.2603-0.29480.0378-0.02850.23240.06560.23850.77880.04010.0560.8169-0.36290.3863-42.00045.56572.3256
143.7911-1.7744-5.09541.27132.29076.86910.09780.30950.0776-0.6745-0.1047-0.4535-0.23030.57280.12870.71680.04040.12660.7021-0.02780.4451-33.34085.85374.5788
152.5488-0.5816-0.7023.74633.0422.4938-0.036-0.2131-0.03050.3761-0.07270.51770.4219-0.07290.2630.89890.3663-0.07321.0511-0.58451.205715.4865-33.613-95.2929
161.3656-1.7676-0.86077.43472.93312.9234-0.04360.3971-0.3072-0.75610.0513-0.19970.28060.0936-0.09240.9539-0.1516-0.11590.7419-0.46110.831-26.8976-18.10225.382
178.3022-4.9906-2.60463.03621.88373.56890.2225-0.33550.22560.3309-0.08980.9125-0.404-0.7397-0.06470.53940.1910.02420.6085-0.06990.677127.5194-95.7657-82.3843
182.3785-0.6711-2.35470.25090.69572.34740.1338-0.3159-0.08310.16010.20360.3595-0.28850.189-0.12660.86710.3511-0.08080.7111-0.3331.021322.5124-34.7544-90.7594
193.6668-3.2385-4.34262.86263.83535.13640.08150.111-0.36760.3282-0.05530.04280.54270.29070.0090.8613-0.1751-0.15991.1223-0.58891.0584-21.5447-21.270610.2128
204.2181-2.8792-1.73266.18784.73847.2728-0.1237-0.63830.36840.4536-0.22460.1998-0.3946-0.19410.25880.46030.0093-0.15570.4788-0.05080.664332.2259-91.8987-75.9767
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND (RESSEQ 1:25)
2X-RAY DIFFRACTION2CHAIN B AND (RESSEQ 1:25)
3X-RAY DIFFRACTION3CHAIN C AND (RESSEQ 1:25)
4X-RAY DIFFRACTION4CHAIN D AND (RESSEQ 1:25)
5X-RAY DIFFRACTION5CHAIN A AND (RESSEQ 26:302)
6X-RAY DIFFRACTION6CHAIN B AND (RESSEQ 26:302)
7X-RAY DIFFRACTION7CHAIN C AND (RESSEQ 26:302)
8X-RAY DIFFRACTION8CHAIN D AND (RESSEQ 26:302)
9X-RAY DIFFRACTION9CHAIN A AND (RESSEQ 326:674)
10X-RAY DIFFRACTION10CHAIN B AND (RESSEQ 326:674)
11X-RAY DIFFRACTION11CHAIN C AND (RESSEQ 326:674)
12X-RAY DIFFRACTION12CHAIN D AND (RESSEQ 326:674)
13X-RAY DIFFRACTION13CHAIN A AND (RESSEQ 303:325)
14X-RAY DIFFRACTION14CHAIN A AND (RESSEQ 675:705)
15X-RAY DIFFRACTION15CHAIN B AND (RESSEQ 303:325)
16X-RAY DIFFRACTION16CHAIN C AND (RESSEQ 303:325)
17X-RAY DIFFRACTION17CHAIN D AND (RESSEQ 303:325)
18X-RAY DIFFRACTION18CHAIN B AND (RESSEQ 675:705)
19X-RAY DIFFRACTION19CHAIN C AND (RESSEQ 675:705)
20X-RAY DIFFRACTION20CHAIN D AND (RESSEQ 675:705)

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