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- PDB-4nxt: Crystal structure of the cytosolic domain of human MiD51 -

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Basic information

Entry
Database: PDB / ID: 4nxt
TitleCrystal structure of the cytosolic domain of human MiD51
ComponentsMitochondrial dynamic protein MID51
KeywordsTRANSFERASE / nucleotidyltransferase / protein-protein interaction / ADP / GDP / mitochondrial fission / mitochondria / membrane-anchored
Function / homology
Function and homology information


mitochondrial fission / positive regulation of mitochondrial fission / positive regulation of protein targeting to membrane / ADP binding / GDP binding / cellular response to hypoxia / mitochondrial outer membrane / mitochondrion / identical protein binding
Similarity search - Function
Mitochondrial dynamics protein MID49/MID51 / : / Mitochondrial dynamics protein MID51-like, C-terminal domain / Beta Polymerase; domain 2 - #90 / Poly(a)-polymerase, middle domain - #40 / Poly(a)-polymerase, middle domain / Mab-21-like, HhH/H2TH-like domain / Mab-21 protein HhH/H2TH-like domain / Mab-21 protein nucleotidyltransferase domain / Mab-21-like ...Mitochondrial dynamics protein MID49/MID51 / : / Mitochondrial dynamics protein MID51-like, C-terminal domain / Beta Polymerase; domain 2 - #90 / Poly(a)-polymerase, middle domain - #40 / Poly(a)-polymerase, middle domain / Mab-21-like, HhH/H2TH-like domain / Mab-21 protein HhH/H2TH-like domain / Mab-21 protein nucleotidyltransferase domain / Mab-21-like / Mab-21 / Beta Polymerase; domain 2 / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Mitochondrial dynamics protein MIEF1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.12 Å
AuthorsRichter, V. / Ryan, M.T. / Kvansakul, M.
CitationJournal: J.Cell Biol. / Year: 2014
Title: Structural and functional analysis of MiD51, a dynamin receptor required for mitochondrial fission.
Authors: Richter, V. / Palmer, C.S. / Osellame, L.D. / Singh, A.P. / Elgass, K. / Stroud, D.A. / Sesaki, H. / Kvansakul, M. / Ryan, M.T.
History
DepositionDec 9, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 25, 2013Provider: repository / Type: Initial release
Revision 1.1Mar 19, 2014Group: Database references
Revision 1.2Feb 28, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Mitochondrial dynamic protein MID51
B: Mitochondrial dynamic protein MID51
C: Mitochondrial dynamic protein MID51
D: Mitochondrial dynamic protein MID51
hetero molecules


Theoretical massNumber of molelcules
Total (without water)156,50017
Polymers155,2914
Non-polymers1,20913
Water9,494527
1
A: Mitochondrial dynamic protein MID51
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,0113
Polymers38,8231
Non-polymers1882
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Mitochondrial dynamic protein MID51
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,9152
Polymers38,8231
Non-polymers921
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: Mitochondrial dynamic protein MID51
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,3837
Polymers38,8231
Non-polymers5616
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: Mitochondrial dynamic protein MID51
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,1915
Polymers38,8231
Non-polymers3684
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)72.720, 78.735, 79.362
Angle α, β, γ (deg.)66.26, 84.93, 64.07
Int Tables number1
Space group name H-MP1

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Components

#1: Protein
Mitochondrial dynamic protein MID51 / Mitochondrial dynamic protein of 51 kDa / Mitochondrial elongation factor 1 / Smith-Magenis ...Mitochondrial dynamic protein of 51 kDa / Mitochondrial elongation factor 1 / Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like


Mass: 38822.656 Da / Num. of mol.: 4 / Fragment: unp residues 119-463
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Gene: candidate 7-like, MID51, MIEF1, SMCR7L, Smith-Magenis syndrome chromosome region
Plasmid: pGEX-4T-1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: Q9NQG6
#2: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C3H8O3
#3: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: SO4
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 527 / Source method: isolated from a natural source / Formula: H2O

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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: 2.4 Å3/Da / Density % sol: 48.65 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 16% PEG 8000, 0.1M HEPES, 10% 2-propanol, 0.2M ammonium sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Sep 21, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
ReflectionResolution: 2.12→40.67 Å / Num. obs: 79550 / % possible obs: 97.3 % / Redundancy: 2.7 % / Biso Wilson estimate: 32 Å2 / Rmerge(I) obs: 0.066 / Net I/σ(I): 11
Reflection shellResolution: 2.12→2.23 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.5 / Mean I/σ(I) obs: 2.8 / Num. unique all: 79550

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Processing

Software
NameVersionClassification
ADSCQuantumdata collection
PHENIXmodel building
PHENIX(phenix.refine: 1.8.4_1496)refinement
XDSdata reduction
SCALAdata scaling
PHENIXphasing
RefinementMethod to determine structure: SAD / Resolution: 2.12→39.007 Å / SU ML: 0.28 / σ(F): 1.96 / Phase error: 28.41 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2626 3964 4.98 %random
Rwork0.2228 ---
obs-79549 97.3 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.12→39.007 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10276 0 75 527 10878
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00410587
X-RAY DIFFRACTIONf_angle_d0.80214442
X-RAY DIFFRACTIONf_dihedral_angle_d13.5913888
X-RAY DIFFRACTIONf_chiral_restr0.0311676
X-RAY DIFFRACTIONf_plane_restr0.0041846
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.12-2.14590.3341480.29952695X-RAY DIFFRACTION97
2.1459-2.1730.31511460.30112651X-RAY DIFFRACTION97
2.173-2.20160.33911420.28892713X-RAY DIFFRACTION97
2.2016-2.23180.33111530.28582715X-RAY DIFFRACTION97
2.2318-2.26360.3291450.28242660X-RAY DIFFRACTION97
2.2636-2.29740.30251320.26622694X-RAY DIFFRACTION98
2.2974-2.33330.26441180.26932781X-RAY DIFFRACTION98
2.3333-2.37160.30491280.25692687X-RAY DIFFRACTION98
2.3716-2.41250.29331510.25372720X-RAY DIFFRACTION98
2.4125-2.45630.30261220.26282724X-RAY DIFFRACTION98
2.4563-2.50360.29591460.25752723X-RAY DIFFRACTION97
2.5036-2.55470.29671460.25362678X-RAY DIFFRACTION98
2.5547-2.61020.27061310.24722771X-RAY DIFFRACTION98
2.6102-2.67090.26831470.23862670X-RAY DIFFRACTION98
2.6709-2.73770.26591450.24962727X-RAY DIFFRACTION98
2.7377-2.81170.27691300.25152757X-RAY DIFFRACTION98
2.8117-2.89440.27811470.23982679X-RAY DIFFRACTION98
2.8944-2.98780.29391490.22992714X-RAY DIFFRACTION98
2.9878-3.09450.2411320.2232708X-RAY DIFFRACTION98
3.0945-3.21840.27951600.22162704X-RAY DIFFRACTION97
3.2184-3.36480.28161460.22332673X-RAY DIFFRACTION97
3.3648-3.5420.25821440.21632683X-RAY DIFFRACTION97
3.542-3.76380.25591390.20072719X-RAY DIFFRACTION97
3.7638-4.05410.23671440.19872628X-RAY DIFFRACTION96
4.0541-4.46160.22551280.18092697X-RAY DIFFRACTION96
4.4616-5.1060.23461460.18752651X-RAY DIFFRACTION96
5.106-6.42830.2761590.22032699X-RAY DIFFRACTION98
6.4283-39.01390.21141390.19752665X-RAY DIFFRACTION96
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)
16.28521.13810.12790.26180.05632.9245-0.0938-0.2647-0.6231-0.5310.1289-0.8750.180.3586-0.1690.37420.03790.1650.5212-0.00460.791112.25734.23485.8776
25.12032.285-5.59651.0147-2.31755.76870.7773-0.80740.07490.1507-0.3703-0.055-0.43090.5116-0.35460.3418-0.06190.03320.391-0.10260.3863-17.046120.894120.2611
35.213-0.0495-5.4993.0704-0.626.8979-0.1739-0.7508-0.34160.0823-0.0249-0.3049-0.02330.70590.25840.2332-0.0355-0.01860.4103-0.11230.3246-17.053711.971817.3156
46.6228-1.281-1.79820.33410.60481.4298-0.31330.536-1.30670.08420.03640.08870.3749-0.01590.32320.4210.00960.09310.372-0.15830.4283-29.1446-2.397813.4213
57.41984.6854-1.37155.7237-0.00674.0956-0.11340.76930.0777-0.13440.12740.29210.0833-0.2355-0.03370.21520.0426-0.03110.421-0.02470.2679-38.59585.47113.3703
63.6519-3.2636-2.58769.1471-0.97363.605-0.02561.12320.3206-1.07390.11120.1623-0.8318-0.4842-0.06370.41640.0283-0.01150.48110.07540.5021-22.204524.851710.6171
73.80071.79720.52826.21641.41393.0544-0.30140.7388-0.0249-0.59930.1632-0.0823-0.02970.09940.07810.23290.03570.02350.4517-0.04940.2479-20.93177.57259.1582
85.11111.0951-1.24353.91870.89863.18450.0293-0.0143-0.5441-0.2008-0.1796-0.68270.07980.15290.1450.29390.03840.11150.3669-0.01190.5574-2.3881-3.64735.1428
97.50261.8717-4.42372.8396-2.96624.68530.2537-0.23790.62070.24330.09160.4963-0.1721-0.1719-0.37930.3018-0.00080.030.3777-0.06790.3249-10.195-22.8962-6.1701
101.79-1.59090.36173.6368-0.46960.9082-0.0625-0.2179-0.4317-0.05220.2730.5567-0.0399-0.2803-0.14340.3063-0.03830.02250.42070.06160.4378-11.8818-42.5878-4.8736
113.36831.6522-1.12163.7953-1.12752.24410.07090.00870.0666-0.0733-0.064-0.0546-0.04250.0678-0.00310.19150.01040.04930.2826-0.00540.2667.9572-26.6505-14.2965
122.639-3.8764-1.75517.93473.18963.73930.146-0.88870.7444-0.12540.6326-1.7541-0.64080.4664-0.67310.4835-0.13480.10210.5898-0.27330.702857.970341.518854.5704
133.8372.7842.51624.37313.60316.77640.2280.2825-0.28760.13230.127-0.58910.42790.4144-0.32570.24260.03050.02970.3810.04570.28653.944316.765337.1498
143.07681.0656-0.58672.2831.64982.1982-0.0570.4349-0.17930.1547-0.05750.26780.2061-0.20650.12520.29480.00590.02010.35090.02160.251531.851710.029536.483
157.67681.47296.71122.27550.65466.09650.4726-0.0605-0.98810.4834-0.0748-0.4840.9399-0.1685-0.35660.47070.0404-0.01840.49170.13810.624557.17926.304944.3181
165.7360.4007-0.11023.14390.51910.57450.0276-0.28590.2490.3289-0.1443-0.35260.1060.2280.06540.3111-0.0063-0.03190.35210.05110.25564616.60945.2112
170.59860.92870.75634.31922.91622.37560.106-0.09520.1481-0.32110.0659-0.1072-0.36960.2526-0.25630.29030.00230.08280.3729-0.01320.362444.412932.330345.3612
182.56191.38710.74758.93020.92124.0850.0526-0.14870.36970.010.05340.4149-0.6070.0256-0.12080.3329-0.02640.10420.2653-0.04240.28838.472239.472948.4136
195.0162.5307-1.94732.62251.24764.13050.5057-0.55860.22471.7685-0.42950.30880.5293-0.145-0.19030.7545-0.05780.03620.4096-0.04760.388441.325137.16163.856
204.0609-5.3507-2.92987.15444.22264.19510.507-0.30291.0666-0.005-0.4391-0.3558-1.22040.0939-0.21680.8647-0.05120.17460.49060.0891.097269.40758.622330.3993
216.8509-4.8837-5.01835.05865.85236.87820.07730.01910.7597-10.5873-0.6604-0.9370.6803-0.76040.6848-0.19210.15650.52940.00130.690894.116545.800215.8047
227.8445-2.7739-2.88135.52292.9344.4306-0.00240.596-0.23670.0128-0.22250.3654-0.3098-0.02180.04570.4985-0.05920.15820.42330.08910.447187.466540.047718.7216
232.8071-1.4056-2.1916.66453.46415.1441-0.08410.0849-0.75880.2662-0.30610.07360.2969-0.00940.28670.26970.06220.03910.4260.04640.589482.547222.107421.7055
244.7288-3.2711-1.3625.41474.5415.9981-0.11820.10230.29891.06820.7843-0.72930.64970.3494-0.47360.45070.16620.1690.51170.12161.006892.869313.626818.7374
252.2914-1.0099-1.94383.5693-0.38352.0424-0.1077-0.1856-0.21960.85050.3844-1.6112-0.40760.8934-0.40070.6173-0.1036-0.05080.8294-0.0641.0621100.670638.638123.3924
267.14764.76882.2183.26141.94586.74330.2871-0.29910.40930.8215-0.1984-0.2078-0.85180.4488-0.03510.6814-0.02530.12180.5311-0.08820.598591.823642.804125.5303
276.27451.19250.8093.24680.63055.7648-0.0685-0.275-0.10280.05850.4486-0.2267-0.3783-0.346-0.38530.4320.03390.14470.43080.01660.432476.532331.798724.2135
286.89082.181.84664.66330.54825.39910.4112-0.01591.5010.0049-0.2247-0.1155-0.5629-0.6-0.34990.52130.08210.2730.41920.10490.857371.271647.371231.8327
294.17960.3497-1.28083.87930.83675.52570.3009-0.15160.89190.2005-0.09810.4465-0.4357-0.2484-0.23610.41950.02410.19490.4547-0.00170.582464.642941.104734.4279
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 125 through 150 )
2X-RAY DIFFRACTION2chain 'A' and (resid 151 through 175 )
3X-RAY DIFFRACTION3chain 'A' and (resid 176 through 200 )
4X-RAY DIFFRACTION4chain 'A' and (resid 201 through 235 )
5X-RAY DIFFRACTION5chain 'A' and (resid 236 through 271 )
6X-RAY DIFFRACTION6chain 'A' and (resid 272 through 296 )
7X-RAY DIFFRACTION7chain 'A' and (resid 297 through 341 )
8X-RAY DIFFRACTION8chain 'A' and (resid 342 through 461 )
9X-RAY DIFFRACTION9chain 'B' and (resid 132 through 200 )
10X-RAY DIFFRACTION10chain 'B' and (resid 201 through 333 )
11X-RAY DIFFRACTION11chain 'B' and (resid 334 through 462 )
12X-RAY DIFFRACTION12chain 'C' and (resid 132 through 150 )
13X-RAY DIFFRACTION13chain 'C' and (resid 151 through 200 )
14X-RAY DIFFRACTION14chain 'C' and (resid 201 through 271 )
15X-RAY DIFFRACTION15chain 'C' and (resid 272 through 296 )
16X-RAY DIFFRACTION16chain 'C' and (resid 297 through 333 )
17X-RAY DIFFRACTION17chain 'C' and (resid 334 through 381 )
18X-RAY DIFFRACTION18chain 'C' and (resid 382 through 439 )
19X-RAY DIFFRACTION19chain 'C' and (resid 440 through 462 )
20X-RAY DIFFRACTION20chain 'D' and (resid 133 through 150 )
21X-RAY DIFFRACTION21chain 'D' and (resid 151 through 175 )
22X-RAY DIFFRACTION22chain 'D' and (resid 176 through 200 )
23X-RAY DIFFRACTION23chain 'D' and (resid 201 through 235 )
24X-RAY DIFFRACTION24chain 'D' and (resid 236 through 258 )
25X-RAY DIFFRACTION25chain 'D' and (resid 259 through 289 )
26X-RAY DIFFRACTION26chain 'D' and (resid 290 through 318 )
27X-RAY DIFFRACTION27chain 'D' and (resid 319 through 356 )
28X-RAY DIFFRACTION28chain 'D' and (resid 357 through 381 )
29X-RAY DIFFRACTION29chain 'D' and (resid 382 through 462 )

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