[English] 日本語
Yorodumi
- PDB-5u8x: Crystal structure of Fe-CAO1 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5u8x
TitleCrystal structure of Fe-CAO1
ComponentsCarotenoid oxygenase 1
KeywordsOXIDOREDUCTASE / beta propeller / dioxygenase / resveratrol / carotenoid oxygenase
Function / homologycarotenoid dioxygenase activity / carotene catabolic process / Carotenoid oxygenase / Retinal pigment epithelial membrane protein / Oxidoreductases; Acting on single donors with incorporation of molecular oxygen (oxygenases); With incorporation of two atoms of oxygen / metal ion binding / BENZOIC ACID / : / Carotenoid cleavage oxygenase 1
Function and homology information
Biological speciesNeurospora crassa OR74A (fungus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.165 Å
AuthorsSui, X. / Palczewski, K. / Banerjee, S. / Kiser, P.D.
Funding support United States, 6items
OrganizationGrant numberCountry
National Institutes of Health/National Eye Institute (NIH/NEI)EY009339 United States
National Institutes of Health/National Eye Institute (NIH/NEI)EY020551 United States
National Institutes of Health/National Cancer Institute (NIH/NCI)CA157735 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM77387 United States
Burroughs Wellcome Fund1015187 United States
Department of Veterans Affairs (VA, United States)BX002683 United States
CitationJournal: Biochemistry / Year: 2017
Title: Structure and Spectroscopy of Alkene-Cleaving Dioxygenases Containing an Atypically Coordinated Non-Heme Iron Center.
Authors: Sui, X. / Weitz, A.C. / Farquhar, E.R. / Badiee, M. / Banerjee, S. / von Lintig, J. / Tochtrop, G.P. / Palczewski, K. / Hendrich, M.P. / Kiser, P.D.
History
DepositionDec 15, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 31, 2017Provider: repository / Type: Initial release
Revision 1.1Jun 21, 2017Group: Database references / Structure summary / Category: citation / citation_author / struct_keywords
Item: _citation.journal_abbrev / _citation.journal_id_ISSN ..._citation.journal_abbrev / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.name / _struct_keywords.text
Revision 1.2Sep 13, 2017Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.3Jan 17, 2018Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Dec 11, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.5Apr 13, 2022Group: Author supporting evidence / Database references / Derived calculations
Category: database_2 / pdbx_audit_support / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id
Revision 2.0Feb 8, 2023Group: Advisory / Atomic model ...Advisory / Atomic model / Author supporting evidence / Data collection / Derived calculations / Experimental preparation / Non-polymer description / Refinement description / Source and taxonomy / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / diffrn / entity / entity_src_gen / exptl_crystal_grow / pdbx_audit_support / pdbx_contact_author / pdbx_entity_instance_feature / pdbx_entity_nonpoly / pdbx_entry_details / pdbx_initial_refinement_model / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / pdbx_struct_sheet_hbond / pdbx_validate_close_contact / pdbx_validate_rmsd_angle / pdbx_validate_torsion / refine / refine_hist / refine_ls_restr / refine_ls_restr_ncs / refine_ls_shell / reflns_shell / software / struct_asym / struct_conn / struct_keywords / struct_ncs_dom / struct_ncs_dom_lim / struct_sheet_range / struct_site / struct_site_gen
Item: _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] ..._atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.id / _atom_site_anisotrop.pdbx_label_asym_id / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _diffrn.pdbx_serial_crystal_experiment / _entity_src_gen.pdbx_gene_src_scientific_name / _exptl_crystal_grow.pdbx_details / _pdbx_audit_support.funding_organization / _pdbx_contact_author.id / _pdbx_contact_author.identifier_ORCID / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.value / _pdbx_struct_sheet_hbond.range_1_auth_comp_id / _pdbx_struct_sheet_hbond.range_1_auth_seq_id / _pdbx_struct_sheet_hbond.range_1_label_comp_id / _pdbx_struct_sheet_hbond.range_1_label_seq_id / _pdbx_struct_sheet_hbond.range_2_auth_comp_id / _pdbx_struct_sheet_hbond.range_2_auth_seq_id / _pdbx_struct_sheet_hbond.range_2_label_comp_id / _pdbx_struct_sheet_hbond.range_2_label_seq_id / _refine.B_iso_mean / _refine.aniso_B[1][1] / _refine.aniso_B[1][2] / _refine.aniso_B[2][2] / _refine.aniso_B[3][3] / _refine.correlation_coeff_Fo_to_Fc / _refine.correlation_coeff_Fo_to_Fc_free / _refine.ls_R_factor_R_free / _refine.ls_R_factor_R_work / _refine.ls_R_factor_obs / _refine.overall_SU_B / _refine.overall_SU_ML / _refine.pdbx_overall_ESU_R / _refine.pdbx_overall_ESU_R_Free / _refine.pdbx_stereochemistry_target_values / _refine.solvent_model_details / _refine_hist.number_atoms_solvent / _refine_hist.number_atoms_total / _refine_hist.pdbx_number_atoms_ligand / _refine_ls_restr.dev_ideal / _refine_ls_restr.dev_ideal_target / _refine_ls_restr.number / _refine_ls_shell.R_factor_R_free / _refine_ls_shell.R_factor_R_work / _refine_ls_shell.d_res_high / _refine_ls_shell.pdbx_total_number_of_bins_used / _reflns_shell.number_unique_obs / _software.version / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_keywords.text / _struct_sheet_range.beg_auth_comp_id / _struct_sheet_range.beg_auth_seq_id / _struct_sheet_range.beg_label_comp_id / _struct_sheet_range.beg_label_seq_id
Description: Ligand geometry
Details: Metal occupancy was refined and the piceatannol dictionary file from CCP4 was used.
Provider: author / Type: Coordinate replacement
Revision 2.1Oct 25, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond
Revision 3.0Jul 10, 2024Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Other / Refinement description / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / atom_sites / entity / pdbx_nonpoly_scheme / pdbx_struct_conn_angle / pdbx_struct_sheet_hbond / pdbx_unobs_or_zero_occ_atoms / pdbx_validate_torsion / refine / refine_hist / refine_ls_restr / refine_ls_restr_ncs / refine_ls_shell / reflns / software / struct_conn / struct_keywords / struct_ncs_dom / struct_ncs_dom_lim / struct_ncs_ens
Item: _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] ..._atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.id / _atom_sites.fract_transf_matrix[2][1] / _atom_sites.fract_transf_matrix[3][2] / _entity.pdbx_number_of_molecules / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _pdbx_struct_sheet_hbond.range_1_auth_comp_id / _pdbx_struct_sheet_hbond.range_1_auth_seq_id / _pdbx_struct_sheet_hbond.range_1_label_comp_id / _pdbx_struct_sheet_hbond.range_1_label_seq_id / _pdbx_struct_sheet_hbond.range_2_auth_comp_id / _pdbx_struct_sheet_hbond.range_2_auth_seq_id / _pdbx_struct_sheet_hbond.range_2_label_comp_id / _pdbx_struct_sheet_hbond.range_2_label_seq_id / _refine.B_iso_mean / _refine.aniso_B[1][1] / _refine.aniso_B[1][2] / _refine.aniso_B[2][2] / _refine.aniso_B[3][3] / _refine.correlation_coeff_Fo_to_Fc_free / _refine.details / _refine.ls_R_factor_R_free / _refine.ls_R_factor_R_work / _refine.ls_R_factor_all / _refine.ls_R_factor_obs / _refine.ls_d_res_high / _refine.ls_d_res_low / _refine.ls_number_reflns_R_work / _refine.ls_number_reflns_obs / _refine.ls_percent_reflns_R_free / _refine.ls_percent_reflns_obs / _refine.overall_SU_B / _refine.overall_SU_ML / _refine.pdbx_overall_ESU_R / _refine.pdbx_overall_ESU_R_Free / _refine.pdbx_stereochemistry_target_values / _refine.solvent_model_details / _refine_hist.cycle_id / _refine_hist.d_res_high / _refine_hist.d_res_low / _refine_hist.number_atoms_solvent / _refine_hist.number_atoms_total / _refine_hist.pdbx_number_atoms_protein / _refine_ls_restr.dev_ideal / _refine_ls_restr.dev_ideal_target / _refine_ls_restr.number / _refine_ls_restr.type / _reflns.d_resolution_high / _software.version / _struct_conn.pdbx_dist_value / _struct_conn.ptnr2_auth_seq_id / _struct_keywords.text
Description: Model completeness
Details: Additional waters of mechanistic relevance were added. An active site site chain conformation was updated.
Provider: author / Type: Coordinate replacement

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Carotenoid oxygenase 1
B: Carotenoid oxygenase 1
C: Carotenoid oxygenase 1
D: Carotenoid oxygenase 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)238,72315
Polymers237,9924
Non-polymers73211
Water20,5731142
1
A: Carotenoid oxygenase 1
D: Carotenoid oxygenase 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)119,3017
Polymers118,9962
Non-polymers3055
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Carotenoid oxygenase 1
C: Carotenoid oxygenase 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)119,4238
Polymers118,9962
Non-polymers4276
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)100.908, 100.908, 448.815
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number154
Space group name H-MP3221
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21A
32A
42A
53A
63A
74A
84A
95A
105A
116A
126A

NCS domain segments:

Beg auth comp-ID: LEU / Beg label comp-ID: LEU / Auth asym-ID: A / Label asym-ID: A

Dom-IDComponent-IDEns-IDEnd auth comp-IDEnd label comp-IDAuth seq-IDLabel seq-ID
111LEULEU30 - 52630 - 526
211LEULEU30 - 52630 - 526
322PROPRO30 - 52530 - 525
422PROPRO30 - 52530 - 525
533LEULEU30 - 52630 - 526
633LEULEU30 - 52630 - 526
744PROPRO30 - 52530 - 525
844PROPRO30 - 52530 - 525
955LEULEU30 - 52630 - 526
1055LEULEU30 - 52630 - 526
1166PROPRO30 - 52530 - 525
1266PROPRO30 - 52530 - 525

NCS ensembles :
IDDetails
1Local NCS retraints between domains: 1 2
2Local NCS retraints between domains: 3 4
3Local NCS retraints between domains: 5 6
4Local NCS retraints between domains: 7 8
5Local NCS retraints between domains: 9 10
6Local NCS retraints between domains: 11 12

-
Components

#1: Protein
Carotenoid oxygenase 1


Mass: 59497.934 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Neurospora crassa OR74A (fungus)
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
Gene: cao-1, NCU07008 / Production host: Escherichia coli (E. coli) / References: UniProt: Q7S860
#2: Chemical
ChemComp-FE2 / FE (II) ION


Mass: 55.845 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Fe / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cl
#4: Chemical ChemComp-BEZ / BENZOIC ACID


Mass: 122.121 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Formula: C7H6O2
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1142 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.77 Å3/Da / Density % sol: 55.62 %
Crystal growTemperature: 281 K / Method: vapor diffusion, hanging drop / Details: Sodium polyacrylate, HEPES, pH 6.5

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 1.722 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Apr 1, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.722 Å / Relative weight: 1
ReflectionResolution: 2.165→50.14 Å / Num. obs: 128129 / % possible obs: 89.8 % / Redundancy: 17.4 % / Rmerge(I) obs: 0.157 / Net I/σ(I): 17
Reflection shellResolution: 2.17→2.3 Å / Redundancy: 7.5 % / Rmerge(I) obs: 1.711 / Mean I/σ(I) obs: 0.93 / Num. unique obs: 12800 / % possible all: 56.2

-
Processing

Software
NameVersionClassification
REFMAC5.8.0415refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4OU9
Resolution: 2.165→50.138 Å / Cor.coef. Fo:Fc: 0.964 / Cor.coef. Fo:Fc free: 0.952 / SU B: 6.22 / SU ML: 0.141 / Cross valid method: THROUGHOUT / ESU R: 0.235 / ESU R Free: 0.176
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflectionSelection details
Rfree0.2055 6323 4.937 %RANDOM
Rwork0.1807 121762 --
all0.182 ---
obs-128085 89.813 %-
Solvent computationIon probe radii: 0.7 Å / Shrinkage radii: 0.7 Å / VDW probe radii: 1.1 Å / Solvent model: MASK BULK SOLVENT
Displacement parametersBiso mean: 40.645 Å2
Baniso -1Baniso -2Baniso -3
1-0.582 Å20.291 Å20 Å2
2--0.582 Å2-0 Å2
3----1.887 Å2
Refinement stepCycle: LAST / Resolution: 2.165→50.138 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms15941 0 35 1142 17118
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0030.01216522
X-RAY DIFFRACTIONr_bond_other_d0.0010.01614974
X-RAY DIFFRACTIONr_angle_refined_deg0.9211.66722468
X-RAY DIFFRACTIONr_angle_other_deg0.3151.58234558
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.17351997
X-RAY DIFFRACTIONr_dihedral_angle_2_deg1.3522.074121
X-RAY DIFFRACTIONr_dihedral_angle_3_deg11.941102546
X-RAY DIFFRACTIONr_dihedral_angle_6_deg14.56110839
X-RAY DIFFRACTIONr_chiral_restr0.0460.22288
X-RAY DIFFRACTIONr_chiral_restr_other0.0160.21
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.0219875
X-RAY DIFFRACTIONr_gen_planes_other0.0010.024009
X-RAY DIFFRACTIONr_nbd_refined0.1860.22750
X-RAY DIFFRACTIONr_symmetry_nbd_other0.1830.213731
X-RAY DIFFRACTIONr_nbtor_refined0.1780.27859
X-RAY DIFFRACTIONr_symmetry_nbtor_other0.0780.28468
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1360.21017
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_other0.1080.21
X-RAY DIFFRACTIONr_metal_ion_refined0.0080.21
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.1310.221
X-RAY DIFFRACTIONr_nbd_other0.2270.272
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.1250.29
X-RAY DIFFRACTIONr_mcbond_it1.924.1957982
X-RAY DIFFRACTIONr_mcbond_other1.924.1957982
X-RAY DIFFRACTIONr_mcangle_it3.0977.5369978
X-RAY DIFFRACTIONr_mcangle_other3.0997.5379979
X-RAY DIFFRACTIONr_scbond_it2.4364.5028540
X-RAY DIFFRACTIONr_scbond_other2.4354.5028541
X-RAY DIFFRACTIONr_scangle_it4.1388.13212489
X-RAY DIFFRACTIONr_scangle_other4.1378.13212490
X-RAY DIFFRACTIONr_lrange_it5.75241.45717924
X-RAY DIFFRACTIONr_lrange_other5.73141.4717859
X-RAY DIFFRACTIONr_ncsr_local_group_10.0540.0516394
X-RAY DIFFRACTIONr_ncsr_local_group_20.050.0516469
X-RAY DIFFRACTIONr_ncsr_local_group_30.0560.0516422
X-RAY DIFFRACTIONr_ncsr_local_group_40.050.0516377
X-RAY DIFFRACTIONr_ncsr_local_group_50.050.0516418
X-RAY DIFFRACTIONr_ncsr_local_group_60.0520.0516396
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDTypeRms dev position (Å)Weight position
11AX-RAY DIFFRACTIONLocal ncs0.053770.05011
12AX-RAY DIFFRACTIONLocal ncs0.053770.05011
23AX-RAY DIFFRACTIONLocal ncs0.050030.05011
24AX-RAY DIFFRACTIONLocal ncs0.050030.05011
35AX-RAY DIFFRACTIONLocal ncs0.05640.0501
36AX-RAY DIFFRACTIONLocal ncs0.05640.0501
47AX-RAY DIFFRACTIONLocal ncs0.049750.05011
48AX-RAY DIFFRACTIONLocal ncs0.049750.05011
59AX-RAY DIFFRACTIONLocal ncs0.050250.0501
510AX-RAY DIFFRACTIONLocal ncs0.050250.0501
611AX-RAY DIFFRACTIONLocal ncs0.052110.0501
612AX-RAY DIFFRACTIONLocal ncs0.052110.0501
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRfactor allNum. reflection allFsc freeFsc work% reflection obs (%)WRfactor Rwork
2.165-2.2210.4192630.41449900.415104160.830.82250.4320.424
2.221-2.2820.3723030.35957610.36101130.9150.91559.96240.354
2.282-2.3480.3453500.32966540.3398890.9430.94270.82620.311
2.348-2.420.334080.32177490.32295300.9330.94385.59290.3
2.42-2.50.2924540.26886260.26993360.9540.96197.25790.237
2.5-2.5870.264430.23584270.23790410.9620.96898.10860.204
2.587-2.6840.2284230.2180340.21186010.9670.97498.32580.18
2.684-2.7940.2454150.21378890.21584240.9640.97498.57550.185
2.794-2.9180.2413870.21175810.21280630.9640.97698.82180.19
2.918-3.0590.2553690.20572920.20777400.9590.97798.97930.186
3.059-3.2240.2363530.19768970.19973120.9630.97999.15210.181
3.224-3.4190.2043360.17765960.17969780.9750.98299.34080.166
3.419-3.6540.1843200.16162270.16365790.980.98599.51360.154
3.654-3.9450.1712980.14457990.14561170.9820.98899.6730.14
3.945-4.3190.1512760.12954030.1356860.9870.9999.87690.128
4.319-4.8240.1392540.11849270.11951840.9890.99299.94210.121
4.824-5.5620.1552270.1343760.13146040.9890.99299.97830.132
5.562-6.7910.1731940.15737510.15839480.9840.98899.9240.157
6.791-9.5170.1481550.14229630.14231180.9870.9881000.149
9.517-50.1380.189950.16818200.16919160.9780.98199.94780.192

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more