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- PDB-4bh6: Insights into degron recognition by APC coactivators from the str... -

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Basic information

Entry
Database: PDB / ID: 4bh6
TitleInsights into degron recognition by APC coactivators from the structure of an Acm1-Cdh1 complex
Components
  • APC/C ACTIVATOR PROTEIN CDH1
  • APC/C-CDH1 MODULATOR 1
KeywordsCELL CYCLE / ANAPHASE PROMOTING COMPLEX / ACM1 / UBIQUITINATION / D BOX
Function / homology
Function and homology information


negative regulation of mitotic spindle pole body separation / Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase / positive regulation of mitotic actomyosin contractile ring contraction / ubiquitin-protein transferase inhibitor activity / deactivation of mitotic spindle assembly checkpoint / positive regulation of anaphase-promoting complex-dependent catabolic process / anaphase-promoting complex / anaphase-promoting complex-dependent catabolic process / anaphase-promoting complex binding / positive regulation of mitotic metaphase/anaphase transition ...negative regulation of mitotic spindle pole body separation / Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase / positive regulation of mitotic actomyosin contractile ring contraction / ubiquitin-protein transferase inhibitor activity / deactivation of mitotic spindle assembly checkpoint / positive regulation of anaphase-promoting complex-dependent catabolic process / anaphase-promoting complex / anaphase-promoting complex-dependent catabolic process / anaphase-promoting complex binding / positive regulation of mitotic metaphase/anaphase transition / ubiquitin ligase activator activity / positive regulation of ubiquitin-dependent protein catabolic process / Antigen processing: Ubiquitination & Proteasome degradation / negative regulation of protein ubiquitination / cyclin binding / positive regulation of protein catabolic process / cell division / nucleus / cytoplasm
Similarity search - Function
Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #2450 / The WD repeat Cdc20/Fizzy family / Anaphase-promoting complex subunit 4, WD40 domain / Anaphase-promoting complex subunit 4 WD40 domain / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / YVTN repeat-like/Quinoprotein amine dehydrogenase / 7 Propeller / Methylamine Dehydrogenase; Chain H / Helix non-globular / Special ...Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #2450 / The WD repeat Cdc20/Fizzy family / Anaphase-promoting complex subunit 4, WD40 domain / Anaphase-promoting complex subunit 4 WD40 domain / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / YVTN repeat-like/Quinoprotein amine dehydrogenase / 7 Propeller / Methylamine Dehydrogenase; Chain H / Helix non-globular / Special / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / Mainly Beta
Similarity search - Domain/homology
APC/C activator protein CDH1 / APC/C-CDH1 modulator 1
Similarity search - Component
Biological speciesSACCHAROMYCES CEREVISIAE (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.9 Å
AuthorsHe, J. / Chao, W.C.H. / Zhang, Z. / Yang, J. / Cronin, N. / Barford, D.
CitationJournal: Mol.Cell / Year: 2013
Title: Insights Into Degron Recognition by Apc/C Coactivators from the Structure of an Acm1-Cdh1 Complex.
Authors: He, J. / Chao, W.C. / Zhang, Z. / Yang, J. / Cronin, N. / Barford, D.
History
DepositionMar 29, 2013Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 5, 2013Provider: repository / Type: Initial release
Revision 1.1Jun 19, 2013Group: Database references
Revision 1.2Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / 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 / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id
Revision 1.3Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: APC/C ACTIVATOR PROTEIN CDH1
B: APC/C ACTIVATOR PROTEIN CDH1
C: APC/C ACTIVATOR PROTEIN CDH1
D: APC/C ACTIVATOR PROTEIN CDH1
E: APC/C ACTIVATOR PROTEIN CDH1
F: APC/C ACTIVATOR PROTEIN CDH1
G: APC/C ACTIVATOR PROTEIN CDH1
H: APC/C ACTIVATOR PROTEIN CDH1
I: APC/C-CDH1 MODULATOR 1
J: APC/C-CDH1 MODULATOR 1
K: APC/C-CDH1 MODULATOR 1
L: APC/C-CDH1 MODULATOR 1
M: APC/C-CDH1 MODULATOR 1
N: APC/C-CDH1 MODULATOR 1
O: APC/C-CDH1 MODULATOR 1
P: APC/C-CDH1 MODULATOR 1


Theoretical massNumber of molelcules
Total (without water)339,30016
Polymers339,30016
Non-polymers00
Water50428
1
D: APC/C ACTIVATOR PROTEIN CDH1
L: APC/C-CDH1 MODULATOR 1


Theoretical massNumber of molelcules
Total (without water)42,4122
Polymers42,4122
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2440 Å2
ΔGint-12.8 kcal/mol
Surface area15450 Å2
MethodPISA
2
H: APC/C ACTIVATOR PROTEIN CDH1
P: APC/C-CDH1 MODULATOR 1


Theoretical massNumber of molelcules
Total (without water)42,4122
Polymers42,4122
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1220 Å2
ΔGint-9.1 kcal/mol
Surface area12650 Å2
MethodPISA
3
A: APC/C ACTIVATOR PROTEIN CDH1
I: APC/C-CDH1 MODULATOR 1


Theoretical massNumber of molelcules
Total (without water)42,4122
Polymers42,4122
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2460 Å2
ΔGint-13.4 kcal/mol
Surface area17360 Å2
MethodPISA
4
C: APC/C ACTIVATOR PROTEIN CDH1
K: APC/C-CDH1 MODULATOR 1


Theoretical massNumber of molelcules
Total (without water)42,4122
Polymers42,4122
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2390 Å2
ΔGint-13.5 kcal/mol
Surface area17230 Å2
MethodPISA
5
B: APC/C ACTIVATOR PROTEIN CDH1
J: APC/C-CDH1 MODULATOR 1


Theoretical massNumber of molelcules
Total (without water)42,4122
Polymers42,4122
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2400 Å2
ΔGint-12.5 kcal/mol
Surface area16870 Å2
MethodPISA
6
E: APC/C ACTIVATOR PROTEIN CDH1
N: APC/C-CDH1 MODULATOR 1


Theoretical massNumber of molelcules
Total (without water)42,4122
Polymers42,4122
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1450 Å2
ΔGint-11.7 kcal/mol
Surface area15700 Å2
MethodPISA
7
F: APC/C ACTIVATOR PROTEIN CDH1
M: APC/C-CDH1 MODULATOR 1


Theoretical massNumber of molelcules
Total (without water)42,4122
Polymers42,4122
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1580 Å2
ΔGint-9.7 kcal/mol
Surface area15950 Å2
MethodPISA
8
G: APC/C ACTIVATOR PROTEIN CDH1
O: APC/C-CDH1 MODULATOR 1


Theoretical massNumber of molelcules
Total (without water)42,4122
Polymers42,4122
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1460 Å2
ΔGint-11.4 kcal/mol
Surface area15760 Å2
MethodPISA
Unit cell
Length a, b, c (Å)198.431, 188.142, 93.440
Angle α, β, γ (deg.)90.00, 92.13, 90.00
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E
61F
71G
81H
12I
22J
32K
42L
13M
23N
33O
43P

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1111A248 - 546
2111B248 - 546
3111C248 - 546
4111D248 - 546
5111E248 - 546
6111F248 - 546
7111G248 - 546
8111H248 - 546
1121I60 - 111
2121J60 - 111
3121K60 - 111
4121L60 - 111
1131M62 - 79
2131N62 - 70
3131O62 - 79
4131P62 - 79

NCS ensembles :
ID
1
2
3

NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(0.998632, 0.013169, 0.050598), (-0.011458, 0.999357, -0.033962), (-0.051013, 0.033336, 0.998141)103.13516, -4.5987, 42.86938
3given(-0.496111, -0.12322, -0.859471), (0.147622, -0.987437, 0.056355), (-0.855618, -0.098919, 0.508068)3.03378, 9.75679, 3.37357
4given(-0.473363, -0.131345, -0.87102), (0.104531, -0.99021, 0.09251), (-0.874643, -0.047258, 0.482458)-86.19245, 25.83005, -61.10667
5given(-0.62529, 0.74494, -0.232545), (-0.778044, -0.61819, 0.111755), (-0.060506, 0.25081, 0.966144)-12.65025, -15.59597, 11.87326
6given(0.563088, -0.698928, 0.440944), (0.29615, 0.6688, 0.68191), (-0.77151, -0.25339, 0.583581)-5.02476, -25.18367, 15.73205
7given(-0.568825, 0.762201, -0.309013), (-0.812253, -0.579612, 0.065527), (-0.129163, 0.28827, 0.948798)-85.48651, -93.51279, 44.11447
8given(0.531323, -0.675022, 0.511899), (0.236734, 0.698479, 0.67534), (-0.81342, -0.23764, 0.530919)72.60971, 31.23273, -39.08913
9given(1), (1), (1)
10given(0.998241, -0.003186, 0.059199), (0.005263, 0.999375, -0.03496), (-0.059051, 0.03521, 0.997634)103.17595, -2.55977, 41.88637
11given(-0.478434, -0.124859, -0.869201), (0.111311, -0.990478, 0.081012), (-0.87104, -0.057993, 0.487777)2.30074, 10.98607, 2.52715
12given(-0.44945, -0.139526, -0.882342), (0.07325, -0.990157, 0.119263), (-0.890297, -0.011028, 0.455247)-84.85048, 24.93556, -64.60947
13given(1), (1), (1)
14given(-0.493656, 0.041288, -0.868677), (-0.070262, -0.9975, -0.007482), (-0.866814, 0.057341, 0.495323)-0.32589, 12.07526, 0.25034
15given(-0.43458, 0.033238, -0.90002), (-0.117133, -0.992917, 0.01989), (-0.892984, 0.114066, 0.435395)-86.61104, 2.85321, -68.25789
16given(0.994951, -0.000963, 0.100359), (0.010256, 0.995695, -0.092126), (-0.099838, 0.09269, 0.990677)104.53623, -5.46042, 37.52433

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Components

#1: Protein
APC/C ACTIVATOR PROTEIN CDH1 / CDH1 / CDC20 HOMOLOG 1 / HOMOLOG OF CDC TWENTY 1


Mass: 34273.637 Da / Num. of mol.: 8 / Fragment: WD40 DOMAIN, RESIDUES 241-548
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast)
Cell line (production host): SF9 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: P53197
#2: Protein
APC/C-CDH1 MODULATOR 1


Mass: 8138.838 Da / Num. of mol.: 8 / Fragment: RESIDUES 59-128
Source method: isolated from a genetically manipulated source
Details: PHOSPORYLATED AT SER 102
Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast)
Cell line (production host): SF9 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: Q08981
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 28 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY
Nonpolymer detailsPHOSPHOSERINE (SEP): SPONTANEOUSLY PHOSPHORYLATED IN INSECT CELL SYSTEM

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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: 2.6 Å3/Da / Density % sol: 58 % / Description: NONE
Crystal growpH: 6 / Details: PEG, pH 6

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 1
DetectorType: ADSC CCD / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.9→93.4 Å / Num. obs: 72799 / % possible obs: 96.2 % / Observed criterion σ(I): 0 / Redundancy: 2.8 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 8
Reflection shellResolution: 2.9→3 Å / Redundancy: 2.9 % / Rmerge(I) obs: 0.55 / Mean I/σ(I) obs: 1.9 / % possible all: 98

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Processing

Software
NameVersionClassification
REFMAC5.7.0029refinement
XDSdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4AEZ
Resolution: 2.9→69.27 Å / Cor.coef. Fo:Fc: 0.924 / Cor.coef. Fo:Fc free: 0.895 / SU B: 42.382 / SU ML: 0.351 / Cross valid method: THROUGHOUT / ESU R Free: 0.429 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT. U VALUES WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.25725 3671 5 %RANDOM
Rwork0.21882 ---
obs0.22075 69120 96.09 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 65.477 Å2
Baniso -1Baniso -2Baniso -3
1-0.8 Å20 Å2-0.18 Å2
2---0.5 Å20 Å2
3----0.29 Å2
Refinement stepCycle: LAST / Resolution: 2.9→69.27 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms21463 0 0 28 21491
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.01921932
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.5611.92829819
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.55852734
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.76924.1381015
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.174153563
X-RAY DIFFRACTIONr_dihedral_angle_4_deg22.43415126
X-RAY DIFFRACTIONr_chiral_restr0.1040.23352
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.02116628
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: tight thermal / Weight position: 0.5

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A23028.26
12B23025.98
13C23026.02
14D23025.72
15E23025.17
16F23025.09
17G230211.95
18H23029.39
21I4107.31
22J4106.46
23K4105.87
24L4105.92
31M12035.49
32N12018.01
33O12035.38
34P12088.37
LS refinement shellResolution: 2.9→2.975 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.383 270 -
Rwork0.315 5222 -
obs--97.81 %
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)
11.4707-0.0323-0.17492.62490.50082.1317-0.04150.0481-0.2277-0.1216-0.13320.22320.2447-0.43390.17470.0477-0.0558-0.01350.29-0.10420.1901-29.435-15.027-18.755
21.1234-0.1880.25412.43151.07451.8387-0.1513-0.0647-0.4124-0.013-0.17610.18670.0455-0.37870.32740.06980.0664-0.01450.2737-0.20660.5102-129.069-14.173-67.834
32.16420.12381.08471.8838-0.18751.81660.0269-0.30150.35940.0855-0.0236-0.0461-0.1754-0.2151-0.00330.1856-0.05190.0790.1554-0.04470.119531.45630.69115.171
42.45040.0781.20451.97130.06193.15850.0617-0.23780.40810.244-0.03410.29680.1-0.4497-0.02760.25450.01490.11470.17490.07550.2361-68.13230.991-32.825
53.89940.4421.03780.6930.54874.76440.31710.5575-0.6116-0.01130.1427-0.12680.53950.9306-0.45980.16670.1846-0.08340.3589-0.18210.151811.889-20.408-25.814
63.05540.02151.14272.4783-0.1592.68910.11690.53740.3966-0.593-0.17860.12020.14020.13290.06170.23350.02110.01010.27540.18020.183915.98132.545-23.985
71.8241-0.4406-0.74460.84180.19721.90670.10830.035-0.09590.0611-0.0281-0.3403-0.04280.3964-0.08020.1087-0.0559-0.05770.1966-0.07720.3235-87.581-20.799-71.947
81.76810.75220.18996.5166-3.03936.75540.06990.51720.6121-1.35071.04611.77090.798-1.0375-1.11610.3395-0.2394-0.37270.60740.57370.7172-81.33331.539-72.822
93.08891.42831.23031.09270.7451.0745-0.2460.2152-0.0301-0.14650.02350.04460.01940.1110.22250.2059-0.03350.03170.2124-0.06040.2459-12.866-15.167-27.027
104.44951.54741.39763.65091.33941.7992-0.12280.408-0.3207-0.54910.0747-0.13-0.29930.12340.0480.20670.06140.08030.1513-0.11120.5359-116.466-22.051-77.564
112.23471.01761.32451.90120.92511.28280.09440.17150.4394-0.1012-0.14720.0978-0.1509-0.05870.05270.3095-0.02130.11860.16840.0840.199929.7329.71-3.49
121.8341-0.70020.57711.0733-0.21781.3596-0.03240.24060.166-0.2808-0.0660.26110.1068-0.07250.09850.4646-0.0961-0.01190.25380.19930.3757-69.06329.402-51.202
133.83586.80651.049112.25641.980.3767-1.37971.0888-0.8351-2.89551.5315-1.382-0.5742-0.0512-0.15182.13950.20510.14542.0213-0.14390.503122.25721.959-45.919
1413.51747.8351-2.79095.44570.9878.1018-0.76450.56670.3907-0.84331.14490.0808-0.90142.0216-0.38030.2884-0.15060.1071.909-0.32740.300629.162-12.376-42.358
1512.074310.38910.62638.95170.54350.0461-0.40970.5729-0.7081-0.38710.4877-0.731-0.12090.0251-0.07790.74550.04880.33411.55570.04241.2201-68.581-13.15-87.493
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A245 - 548
2X-RAY DIFFRACTION2B245 - 548
3X-RAY DIFFRACTION3C245 - 548
4X-RAY DIFFRACTION4D244 - 548
5X-RAY DIFFRACTION5E246 - 548
6X-RAY DIFFRACTION6F245 - 548
7X-RAY DIFFRACTION7G245 - 547
8X-RAY DIFFRACTION8H248 - 546
9X-RAY DIFFRACTION9I60 - 125
10X-RAY DIFFRACTION10J60 - 125
11X-RAY DIFFRACTION11K60 - 125
12X-RAY DIFFRACTION12L60 - 111
13X-RAY DIFFRACTION13M60 - 80
14X-RAY DIFFRACTION14N60 - 79
15X-RAY DIFFRACTION15O60 - 79

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