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- PDB-7c3f: Crystal structure of ferredoxin: thioredoxin reductase and thiore... -

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Basic information

Entry
Database: PDB / ID: 7c3f
TitleCrystal structure of ferredoxin: thioredoxin reductase and thioredoxin m2 complex
Components
  • (Ferredoxin-thioredoxin reductase ...) x 2
  • Thioredoxin M2, chloroplastic
KeywordsELECTRON TRANSPORT / FTR / Trx m2
Function / homology
Function and homology information


ferredoxin-thioredoxin reductase activity / ferredoxin:thioredoxin reductase / oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor / oxidoreductase activity, acting on iron-sulfur proteins as donors / glycerol ether metabolic process / protein-disulfide reductase (NAD(P)H) activity / thylakoid / chloroplast envelope / chloroplast stroma / positive regulation of catalytic activity ...ferredoxin-thioredoxin reductase activity / ferredoxin:thioredoxin reductase / oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor / oxidoreductase activity, acting on iron-sulfur proteins as donors / glycerol ether metabolic process / protein-disulfide reductase (NAD(P)H) activity / thylakoid / chloroplast envelope / chloroplast stroma / positive regulation of catalytic activity / chloroplast thylakoid membrane / protein-disulfide reductase activity / enzyme activator activity / photosynthesis / chloroplast / cell redox homeostasis / 4 iron, 4 sulfur cluster binding / electron transfer activity / metal ion binding / cytosol / cytoplasm
Similarity search - Function
Ferredoxin thioredoxin reductase, alpha chain / Ferredoxin-thioredoxin reductase, variable chain / Ferredoxin thioredoxin reductase variable alpha chain / Ferredoxin thioredoxin reductase catalytic beta subunit / Ferredoxin thioredoxin reductase catalytic beta subunit superfamily / Ferredoxin thioredoxin reductase catalytic beta chain / Thioredoxin / Electron transport accessory-like domain superfamily / Thioredoxin / Thioredoxin, conserved site ...Ferredoxin thioredoxin reductase, alpha chain / Ferredoxin-thioredoxin reductase, variable chain / Ferredoxin thioredoxin reductase variable alpha chain / Ferredoxin thioredoxin reductase catalytic beta subunit / Ferredoxin thioredoxin reductase catalytic beta subunit superfamily / Ferredoxin thioredoxin reductase catalytic beta chain / Thioredoxin / Electron transport accessory-like domain superfamily / Thioredoxin / Thioredoxin, conserved site / Thioredoxin family active site. / Thioredoxin domain profile. / Thioredoxin domain / Thioredoxin-like superfamily
Similarity search - Domain/homology
IRON/SULFUR CLUSTER / Ferredoxin-thioredoxin reductase subunit A2, chloroplastic / Thioredoxin M2, chloroplastic / Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3986 Å
AuthorsKurisu, G. / Juniar, L. / Tanaka, H.
Funding support Japan, 1items
OrganizationGrant numberCountry
Japan Society for the Promotion of Science (JSPS)16H06560 Japan
CitationJournal: Protein Sci. / Year: 2020
Title: Structural basis for thioredoxin isoform-based fine-tuning of ferredoxin-thioredoxin reductase activity.
Authors: Juniar, L. / Tanaka, H. / Yoshida, K. / Hisabori, T. / Kurisu, G.
History
DepositionMay 12, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Oct 14, 2020Provider: repository / Type: Initial release
Revision 1.1Dec 2, 2020Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title
Revision 1.2Nov 29, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
B: Ferredoxin-thioredoxin reductase variable chain, chloroplastic
C: Thioredoxin M2, chloroplastic
D: Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
E: Ferredoxin-thioredoxin reductase variable chain, chloroplastic
F: Thioredoxin M2, chloroplastic
G: Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
H: Ferredoxin-thioredoxin reductase variable chain, chloroplastic
I: Thioredoxin M2, chloroplastic
J: Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
K: Ferredoxin-thioredoxin reductase variable chain, chloroplastic
L: Thioredoxin M2, chloroplastic
M: Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
N: Ferredoxin-thioredoxin reductase variable chain, chloroplastic
O: Thioredoxin M2, chloroplastic
P: Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
Q: Ferredoxin-thioredoxin reductase variable chain, chloroplastic
R: Thioredoxin M2, chloroplastic
S: Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
T: Ferredoxin-thioredoxin reductase variable chain, chloroplastic
U: Thioredoxin M2, chloroplastic
W: Thioredoxin M2, chloroplastic
V: Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
hetero molecules


Theoretical massNumber of molelcules
Total (without water)294,85540
Polymers292,16423
Non-polymers2,69117
Water9,548530
1
A: Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
B: Ferredoxin-thioredoxin reductase variable chain, chloroplastic
C: Thioredoxin M2, chloroplastic
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,4916
Polymers38,0933
Non-polymers3983
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
D: Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
E: Ferredoxin-thioredoxin reductase variable chain, chloroplastic
F: Thioredoxin M2, chloroplastic
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,4916
Polymers38,0933
Non-polymers3983
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
G: Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
H: Ferredoxin-thioredoxin reductase variable chain, chloroplastic
I: Thioredoxin M2, chloroplastic
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,4685
Polymers38,0933
Non-polymers3752
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
J: Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
K: Ferredoxin-thioredoxin reductase variable chain, chloroplastic
L: Thioredoxin M2, chloroplastic
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,4916
Polymers38,0933
Non-polymers3983
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
M: Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
N: Ferredoxin-thioredoxin reductase variable chain, chloroplastic
O: Thioredoxin M2, chloroplastic
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,4916
Polymers38,0933
Non-polymers3983
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
P: Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
Q: Ferredoxin-thioredoxin reductase variable chain, chloroplastic
R: Thioredoxin M2, chloroplastic
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,4685
Polymers38,0933
Non-polymers3752
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
7
S: Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
T: Ferredoxin-thioredoxin reductase variable chain, chloroplastic
U: Thioredoxin M2, chloroplastic
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,4454
Polymers38,0933
Non-polymers3521
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
8
W: Thioredoxin M2, chloroplastic
V: Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic


Theoretical massNumber of molelcules
Total (without water)25,5102
Polymers25,5102
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)174.262, 137.209, 192.457
Angle α, β, γ (deg.)90.000, 90.210, 90.000
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 3 through 98 or resid 100 through 115 or resid 399))
21(chain D and (resid 3 through 98 or resid 100 through 115 or resid 399))
31(chain G and (resid 3 through 98 or resid 100 through 115 or resid 399))
41(chain J and (resid 3 through 98 or resid 100 through 115 or resid 399))
51(chain M and (resid 3 through 98 or resid 100 through 115 or resid 399))
61(chain P and (resid 3 through 115 or resid 399))
71(chain S and (resid 3 through 98 or resid 100 through 115 or resid 399))
12(chain B and (resid 24 through 107 or resid 109 through 111))
22(chain E and (resid 24 through 107 or resid 109 through 111))
32(chain H and (resid 24 through 107 or resid 109 through 111))
42(chain K and (resid 24 through 107 or resid 109 through 111))
52(chain N and (resid 24 through 107 or resid 109 through 111))
62(chain Q and (resid 24 through 107 or resid 109 through 111))
72chain T
13(chain C and (resid 16 through 68 or resid 70...
23(chain F and (resid 16 through 68 or resid 70...
33(chain I and (resid 16 through 68 or resid 70...
43(chain L and (resid 16 through 68 or resid 70...
53(chain O and (resid 16 through 68 or resid 70...
63(chain R and (resid 16 through 68 or resid 70...
73(chain U and (resid 16 through 68 or resid 70...
83chain W

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 3 through 98 or resid 100 through 115 or resid 399))A3 - 98
121(chain A and (resid 3 through 98 or resid 100 through 115 or resid 399))A100 - 115
131(chain A and (resid 3 through 98 or resid 100 through 115 or resid 399))A399
211(chain D and (resid 3 through 98 or resid 100 through 115 or resid 399))D3 - 98
221(chain D and (resid 3 through 98 or resid 100 through 115 or resid 399))D100 - 115
231(chain D and (resid 3 through 98 or resid 100 through 115 or resid 399))D399
311(chain G and (resid 3 through 98 or resid 100 through 115 or resid 399))G3 - 98
321(chain G and (resid 3 through 98 or resid 100 through 115 or resid 399))G100 - 115
331(chain G and (resid 3 through 98 or resid 100 through 115 or resid 399))G399
411(chain J and (resid 3 through 98 or resid 100 through 115 or resid 399))J3 - 98
421(chain J and (resid 3 through 98 or resid 100 through 115 or resid 399))J100 - 115
431(chain J and (resid 3 through 98 or resid 100 through 115 or resid 399))J399
511(chain M and (resid 3 through 98 or resid 100 through 115 or resid 399))M3 - 98
521(chain M and (resid 3 through 98 or resid 100 through 115 or resid 399))M100 - 115
531(chain M and (resid 3 through 98 or resid 100 through 115 or resid 399))M399
611(chain P and (resid 3 through 115 or resid 399))P0
711(chain S and (resid 3 through 98 or resid 100 through 115 or resid 399))S3 - 98
721(chain S and (resid 3 through 98 or resid 100 through 115 or resid 399))S100 - 115
731(chain S and (resid 3 through 98 or resid 100 through 115 or resid 399))S399
112(chain B and (resid 24 through 107 or resid 109 through 111))B24 - 107
122(chain B and (resid 24 through 107 or resid 109 through 111))B109 - 111
212(chain E and (resid 24 through 107 or resid 109 through 111))E24 - 107
222(chain E and (resid 24 through 107 or resid 109 through 111))E109 - 111
312(chain H and (resid 24 through 107 or resid 109 through 111))H24 - 107
322(chain H and (resid 24 through 107 or resid 109 through 111))H109 - 111
412(chain K and (resid 24 through 107 or resid 109 through 111))K24 - 107
422(chain K and (resid 24 through 107 or resid 109 through 111))K109 - 111
512(chain N and (resid 24 through 107 or resid 109 through 111))N24 - 107
522(chain N and (resid 24 through 107 or resid 109 through 111))N109 - 111
612(chain Q and (resid 24 through 107 or resid 109 through 111))Q24 - 107
622(chain Q and (resid 24 through 107 or resid 109 through 111))Q109 - 111
712chain TT24 - 111
113(chain C and (resid 16 through 68 or resid 70...C16 - 68
123(chain C and (resid 16 through 68 or resid 70...C70 - 84
133(chain C and (resid 16 through 68 or resid 70...C87 - 113
143(chain C and (resid 16 through 68 or resid 70...C115 - 116
153(chain C and (resid 16 through 68 or resid 70...C118
213(chain F and (resid 16 through 68 or resid 70...F16 - 68
223(chain F and (resid 16 through 68 or resid 70...F70 - 84
233(chain F and (resid 16 through 68 or resid 70...F87 - 113
243(chain F and (resid 16 through 68 or resid 70...F115 - 116
253(chain F and (resid 16 through 68 or resid 70...F118
313(chain I and (resid 16 through 68 or resid 70...I16 - 68
323(chain I and (resid 16 through 68 or resid 70...I70 - 84
333(chain I and (resid 16 through 68 or resid 70...I87 - 113
343(chain I and (resid 16 through 68 or resid 70...I115 - 116
353(chain I and (resid 16 through 68 or resid 70...I118
413(chain L and (resid 16 through 68 or resid 70...L16 - 68
423(chain L and (resid 16 through 68 or resid 70...L70 - 84
433(chain L and (resid 16 through 68 or resid 70...L87 - 113
443(chain L and (resid 16 through 68 or resid 70...L115 - 116
453(chain L and (resid 16 through 68 or resid 70...L118
513(chain O and (resid 16 through 68 or resid 70...O16 - 68
523(chain O and (resid 16 through 68 or resid 70...O70 - 84
533(chain O and (resid 16 through 68 or resid 70...O87 - 113
543(chain O and (resid 16 through 68 or resid 70...O115 - 116
553(chain O and (resid 16 through 68 or resid 70...O118
613(chain R and (resid 16 through 68 or resid 70...R16 - 68
623(chain R and (resid 16 through 68 or resid 70...R70 - 84
633(chain R and (resid 16 through 68 or resid 70...R87 - 113
643(chain R and (resid 16 through 68 or resid 70...R115 - 116
653(chain R and (resid 16 through 68 or resid 70...R118
713(chain U and (resid 16 through 68 or resid 70...U16 - 68
723(chain U and (resid 16 through 68 or resid 70...U70 - 84
733(chain U and (resid 16 through 68 or resid 70...U87 - 113
743(chain U and (resid 16 through 68 or resid 70...U115 - 116
753(chain U and (resid 16 through 68 or resid 70...U118
813chain WW10 - 112

NCS ensembles :
ID
1
2
3
DetailsThe crystal contact is not so tight packed and there is space which is enough for two molecules and they turned out to be FTR catalytic (FTRC) and Trxm2cs.

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Components

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Ferredoxin-thioredoxin reductase ... , 2 types, 15 molecules ADGJMPSVBEHKNQT

#1: Protein
Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic / FTR-C / Ferredoxin-thioredoxin reductase subunit B / FTR-B


Mass: 12995.734 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Cell: chloroplast / Gene: FTRC / Plasmid: pETDUET1 / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21
References: UniProt: Q9SJ89, ferredoxin:thioredoxin reductase
#2: Protein
Ferredoxin-thioredoxin reductase variable chain, chloroplastic / Ferredoxin/thioredoxin reductase subunit A (Variable subunit) 2 / Putative lipoic acid synthase


Mass: 12583.467 Da / Num. of mol.: 7
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Cell: chloroplast
Gene: FTRA2, ferredoxin, At5g08410, At5g08410/F8L15_140, C24_LOCUS21561, F8L15.14
Plasmid: pETDUET1 / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q8LBP6

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Protein , 1 types, 8 molecules CFILORUW

#3: Protein
Thioredoxin M2, chloroplastic / AtTrxm2


Mass: 12514.233 Da / Num. of mol.: 8 / Mutation: C41S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Cell: Chloroplast / Gene: TRXM2, At4g03520, F9H3.15, T5L23.1 / Plasmid: pET23 / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q9SEU8

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Non-polymers , 3 types, 547 molecules

#4: Chemical
ChemComp-SF4 / IRON/SULFUR CLUSTER / Iron–sulfur cluster


Mass: 351.640 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: Fe4S4 / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical
ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: Na
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 530 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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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: 3.94 Å3/Da / Density % sol: 71.9 %
Crystal growTemperature: 277.15 K / Method: vapor diffusion, hanging drop / pH: 6.2 / Details: 100 mM NaCitrate pH 6.2 18% PEG 3,350 / PH range: 6.2-7.5

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: NSRRC / Beamline: TPS 05A / Wavelength: 1 Å
DetectorType: RAYONIX MX300-HS / Detector: CCD / Date: Mar 5, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.3986→43.5724 Å / Num. obs: 175388 / % possible obs: 99.14 % / Redundancy: 3.8 % / CC1/2: 0.995 / CC star: 0.999 / Rmerge(I) obs: 0.1234 / Rpim(I) all: 0.07366 / Rrim(I) all: 0.1439 / Net I/σ(I): 8.82
Reflection shellResolution: 2.3986→2.485 Å / Redundancy: 3.8 % / Rmerge(I) obs: 1.406 / Mean I/σ(I) obs: 1.19 / Num. unique obs: 17050 / CC1/2: 0.493 / CC star: 0.813 / Rpim(I) all: 0.83 / Rrim(I) all: 1.635 / % possible all: 96.86

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Processing

Software
NameVersionClassification
PHENIX1.14_3260refinement
PDB_EXTRACT3.25data extraction
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2puk

2puk


Resolution: 2.3986→43.5724 Å / SU ML: 0.35 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 26.95 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2447 8764 5 %
Rwork0.2095 166512 -
obs0.2112 175276 99.09 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 172.48 Å2 / Biso mean: 67.2192 Å2 / Biso min: 27.08 Å2
Refinement stepCycle: final / Resolution: 2.3986→43.5724 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms18397 0 66 530 18993
Biso mean--46.26 55.32 -
Num. residues----2328
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A2352X-RAY DIFFRACTION11.894TORSIONAL
12D2352X-RAY DIFFRACTION11.894TORSIONAL
13G2352X-RAY DIFFRACTION11.894TORSIONAL
14J2352X-RAY DIFFRACTION11.894TORSIONAL
15M2352X-RAY DIFFRACTION11.894TORSIONAL
16P2352X-RAY DIFFRACTION11.894TORSIONAL
17S2352X-RAY DIFFRACTION11.894TORSIONAL
21B1813X-RAY DIFFRACTION11.894TORSIONAL
22E1813X-RAY DIFFRACTION11.894TORSIONAL
23H1813X-RAY DIFFRACTION11.894TORSIONAL
24K1813X-RAY DIFFRACTION11.894TORSIONAL
25N1813X-RAY DIFFRACTION11.894TORSIONAL
26Q1813X-RAY DIFFRACTION11.894TORSIONAL
27T1813X-RAY DIFFRACTION11.894TORSIONAL
31C2229X-RAY DIFFRACTION11.894TORSIONAL
32F2229X-RAY DIFFRACTION11.894TORSIONAL
33I2229X-RAY DIFFRACTION11.894TORSIONAL
34L2229X-RAY DIFFRACTION11.894TORSIONAL
35O2229X-RAY DIFFRACTION11.894TORSIONAL
36R2229X-RAY DIFFRACTION11.894TORSIONAL
37U2229X-RAY DIFFRACTION11.894TORSIONAL
38W2229X-RAY DIFFRACTION11.894TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.3986-2.42580.35672620.3368496989
2.4258-2.45440.36352940.33135589100
2.4544-2.48430.37012920.31285553100
2.4843-2.51580.3282930.3069555599
2.5158-2.54880.33482910.29375525100
2.5488-2.58380.33052940.30015590100
2.5838-2.62070.35922910.29595543100
2.6207-2.65980.34192910.27655529100
2.6598-2.70130.30572970.26635626100
2.7013-2.74560.30612910.2655546100
2.7456-2.7930.31072930.26175553100
2.793-2.84370.31192950.26595603100
2.8437-2.89840.28652910.25965530100
2.8984-2.95760.31142930.25725567100
2.9576-3.02190.29142940.24355592100
3.0219-3.09210.27982950.22555594100
3.0921-3.16940.25222950.22285607100
3.1694-3.25510.26862930.225565100
3.2551-3.35090.27652930.23545584100
3.3509-3.4590.262930.22395550100
3.459-3.58250.25422940.2155590100
3.5825-3.72590.24592920.19695554100
3.7259-3.89540.21032930.1866556299
3.8954-4.10060.21612940.18559699
4.1006-4.35730.20712930.1704555899
4.3573-4.69340.20052920.1699554899
4.6934-5.1650.20762930.1716556799
5.165-5.91080.21082960.1847561799
5.9108-7.4410.20672950.1908561999
7.441-43.57240.1962910.1731553196

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