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- PDB-1w7c: PPLO at 1.23 Angstroms -

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Basic information

Entry
Database: PDB / ID: 1w7c
TitlePPLO at 1.23 Angstroms
ComponentsLYSYL OXIDASE
KeywordsOXIDOREDUCTASE / AMINE OXIDASE / QUINOPROTEIN / TOPAQUINONE ENZYME
Function / homology
Function and homology information


Oxidoreductases; Acting on the CH-NH2 group of donors; With oxygen as acceptor / diamine oxidase activity / cellular response to inorganic substance / primary amine oxidase activity / amine metabolic process / quinone binding / copper ion binding
Similarity search - Function
Domain of unknown function DUF1965 / Domain of unknown function (DUF1965) / Copper amine oxidase, N2-terminal / Copper amine oxidase, N2 domain / Copper amine oxidase, catalytic domain / Nuclear Transport Factor 2; Chain: A, - #40 / Copper amine oxidase / Copper amine oxidase, catalytic domain / Copper amine oxidase, N-terminal / Copper amine oxidase, catalytic domain superfamily ...Domain of unknown function DUF1965 / Domain of unknown function (DUF1965) / Copper amine oxidase, N2-terminal / Copper amine oxidase, N2 domain / Copper amine oxidase, catalytic domain / Nuclear Transport Factor 2; Chain: A, - #40 / Copper amine oxidase / Copper amine oxidase, catalytic domain / Copper amine oxidase, N-terminal / Copper amine oxidase, catalytic domain superfamily / Copper amine oxidase, enzyme domain / Beta-galactosidase; Chain A, domain 5 / Nuclear Transport Factor 2; Chain: A, / Distorted Sandwich / Roll / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
COPPER (II) ION / IMIDAZOLE / Amine oxidase
Similarity search - Component
Biological speciesPICHIA PASTORIS (fungus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.23 Å
AuthorsDuff, A.P. / Cohen, A.E. / Ellis, P.J. / Guss, J.M.
CitationJournal: Acta Crystallogr.,Sect.D / Year: 2006
Title: The 1.23 A Structure of Pichia Pastoris Lysyl Oxidase Reveals a Lysine-Lysine Cross-Link
Authors: Duff, A.P. / Cohen, A.E. / Ellis, P.J. / Hilmer, K. / Langley, D.B. / Dooley, D.M. / Freeman, H.C. / Guss, J.M.
History
DepositionSep 1, 2004Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 31, 2006Provider: repository / Type: Initial release
Revision 1.1Jan 16, 2013Group: Atomic model / Database references ...Atomic model / Database references / Derived calculations / Non-polymer description / Other / Refinement description / Source and taxonomy / Structure summary / Version format compliance
Revision 1.2Jan 30, 2019Group: Advisory / Data collection ...Advisory / Data collection / Experimental preparation / Other
Category: database_PDB_rev / database_PDB_rev_record ...database_PDB_rev / database_PDB_rev_record / exptl_crystal_grow / pdbx_database_proc / pdbx_database_status / pdbx_unobs_or_zero_occ_atoms / struct_biol
Item: _exptl_crystal_grow.method / _exptl_crystal_grow.temp / _pdbx_database_status.recvd_author_approval
Revision 1.3Oct 30, 2019Group: Data collection / Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_conn_angle / struct_conn
Item: _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_comp_id ..._pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.ptnr3_symmetry / _pdbx_struct_conn_angle.value
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.occupancy / _atom_site.type_symbol / _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_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.type_symbol / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.src_method / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_symmetry / _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.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_ptnr1_label_alt_id / _struct_conn.pdbx_role / _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 / _struct_conn.ptnr2_symmetry
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Dec 13, 2023Group: Advisory / Data collection ...Advisory / Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_unobs_or_zero_occ_atoms
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: LYSYL OXIDASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)87,27220
Polymers85,2891
Non-polymers1,98319
Water18,8441046
1
A: LYSYL OXIDASE
hetero molecules

A: LYSYL OXIDASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)174,54440
Polymers170,5782
Non-polymers3,96638
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_655-x+1,y,-z1
Buried area23930 Å2
ΔGint-216.7 kcal/mol
Surface area50370 Å2
MethodPISA
Unit cell
Length a, b, c (Å)139.948, 67.027, 108.688
Angle α, β, γ (deg.)90.00, 118.95, 90.00
Int Tables number5
Space group name H-MC121

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Components

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Protein , 1 types, 1 molecules A

#1: Protein LYSYL OXIDASE /


Mass: 85289.125 Da / Num. of mol.: 1 / Fragment: PPLO HOMOLENZYME HALF DIMER, RESIDUES 41-787
Source method: isolated from a genetically manipulated source
Details: RESIDUE A478 AN ACTIVE SITE TYR RESIDUE, WAS AUTOCATALYTICALLY MODIFIED TO TPQ. THE ENZYME IS GLYCOSYLATED AT ASN A81, ASN A104, ASN A191, ASN A309, AND ASN A 434. RESIDUE LYS 66 IS ...Details: RESIDUE A478 AN ACTIVE SITE TYR RESIDUE, WAS AUTOCATALYTICALLY MODIFIED TO TPQ. THE ENZYME IS GLYCOSYLATED AT ASN A81, ASN A104, ASN A191, ASN A309, AND ASN A 434. RESIDUE LYS 66 IS PARTIALLY CROSS-LINKED WITH RESIDUE LYS 778 TO FORM DEHYDROLYSINONORLEUCINE
Source: (gene. exp.) PICHIA PASTORIS (fungus)
Description: ISOLATION EXUDATE OF OAK, FRANCE HISTORY, ATCC, CBS, A.GUILLIERMOND
Cell line (production host): GS115 / Production host: PICHIA PASTORIS (fungus) / References: UniProt: Q96X16, protein-lysine 6-oxidase

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Sugars , 2 types, 5 molecules

#2: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#8: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 6 types, 1060 molecules

#3: Chemical ChemComp-CU / COPPER (II) ION / Copper


Mass: 63.546 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cu
#4: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#5: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Mg
#6: Chemical
ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Cl
#7: Chemical ChemComp-IMD / IMIDAZOLE / Imidazole


Mass: 69.085 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H5N2
#9: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1046 / Source method: isolated from a natural source / Formula: H2O

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Details

Compound detailsCATALYTIC ACTIVITY: RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2 THE TPQ SIDE CHAIN IS POORLY RESOLVED, ...CATALYTIC ACTIVITY: RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2 THE TPQ SIDE CHAIN IS POORLY RESOLVED, BUT IS DEFINATELY ON-COPPER WITH SIGNIFICANT OCCUPANCY, ESTIMATED 70%, AND IS OFF-COPPER OTHERWISE. THE OFF COPPER STATES ARE NOT RESOLVED.
Sequence detailsRESIDUES 1-40 ARE CLEAVED, AS CONFIRMED BY N-TERMINAL PROTEIN SEQUENCING. NINE SEQUENCE CONFLICTS ...RESIDUES 1-40 ARE CLEAVED, AS CONFIRMED BY N-TERMINAL PROTEIN SEQUENCING. NINE SEQUENCE CONFLICTS ARE MODELLED. RESIDUE Y478 IS POST TRANSLATIONALLY SELF-PROCESSED MODIFIED TO BECOME TPQ. SIGNIFICANT UNINTERPRETED DIFFERENCE DENSITY REMAINS ASSOCIATED WITH THE TPQ SIDE CHAIN. SOME SURFACE SIDE CHAINS THAT ARE COMPLETELY UNOBSERVED HAVE BEEN MODELLED WITH AN OCCUPANCY OF 0.01. THE N-TERMINUS IS RESIDUE 41. RESIDUES 41-42 ARE UNOBSERVED. THE C-TERMINUS FROM RESIDUE 770 SPLITS INTO TWO CONFORMATIONS BEFORE EACH BECOMES UNOBSERVED. ONE CONFORMATION BECOMES UNOBSERVED AFTER RESIDUE 772, THE OTHER BECOMES UNOBSERVED AT RESIDUE 779. THE C-TERMINUS IS RESIDUE 787. MICROHETEROGENEITY IS SUSPECTED AT RESIDUES 337, 362, 413, 469, 498 AND 618, BUT THIS HAS NOT BEEN MODELLED. A PARTIAL CROSS-LINK IS OBSERVED BETWEEN LYS 66 AND LYS 778. THIS CROSS-LINK IS NAMED IN THE PUBLICATION AS DEHYDROLYSINONORLEUCINE KNK 778. THE FORMATION OF THE CROSS- LINK INVOLVES OXIDATION OF ALYS A 778 TO AN ALLYSINE, WHICH REACTS WITH ALYS A 66 TO FORM DEHYDROLYSINONORLEUCINE. IN THIS PROCESS, ALYS A 778 NZ IS LOST AND A DOUBLE BOND IS FORMED BETWEEN ALYS A 66 NZ AND ALYS A 778 CE.

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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: 2.74 Å3/Da / Density % sol: 55.18 %
Crystal growTemperature: 300 K / Method: vapor diffusion, hanging drop / pH: 8
Details: 35% MPD, IMIDAZOLE PH 8.0, 200 MILLIMOLAR MGCL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 300K.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL9-2 / Wavelength: 0.979805
DetectorType: ADSC CCD / Detector: CCD / Date: Apr 1, 2003 / Details: DOUBLE CRYSTAL MONOCHROMATOR
RadiationMonochromator: DOUBLE CRYSTAL MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979805 Å / Relative weight: 1
ReflectionResolution: 1.24→24 Å / Num. obs: 272737 / % possible obs: 95.4 % / Observed criterion σ(I): -3 / Redundancy: 2.78 % / Biso Wilson estimate: 14.06 Å2 / Rmerge(I) obs: 0.04 / Net I/σ(I): 12.77
Reflection shellResolution: 1.23→1.27 Å / Redundancy: 2.1 % / Rmerge(I) obs: 0.512 / Mean I/σ(I) obs: 2.1 / Rsym value: 0.394 / % possible all: 94.8

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Processing

Software
NameVersionClassification
REFMAC5.1.24refinement
MOSFLMdata reduction
SCALAdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1N9E

1n9e


Resolution: 1.23→24.01 Å / Cor.coef. Fo:Fc: 0.988 / Cor.coef. Fo:Fc free: 0.982 / SU B: 0.674 / SU ML: 0.027 / Cross valid method: THROUGHOUT / ESU R: 0.029 / ESU R Free: 0.032 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. COORDINATES FOR THE UNOBSERVED TPQ 478 SIDE CHAIN HAVE BEEN MODELLED, WITH ZERO OCCUPANCY, IN THE STANDARD ON-COPPER CONFORMATION AS ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. COORDINATES FOR THE UNOBSERVED TPQ 478 SIDE CHAIN HAVE BEEN MODELLED, WITH ZERO OCCUPANCY, IN THE STANDARD ON-COPPER CONFORMATION AS ALTERNATE CONFORMER A AND IN THE STANDARD OFF-COPPER CONFORMATION AS ALTERNATE CONFORMATION B. THE B-FACTORS ARE SET TO 50.00, BECAUSE THE APPARENTLY REFINED VALUES WERE INAPPROPRIATE. THE COORDINATES HAVE BEEN CAREFULLY MODELLED. THEY ARE REFINED IN TERMS OF STEREOCHEMISTRY BUT NOT USING X-RAY DATA. THEY ARE DESCRIBED AND ILLUSTRATED IN THE PAPER UNDER REVIEW. THE AUTHORS BELIEVE THAT IN THIS CASE THESE COORDINATES SHOULD APPEAR AS ABOVE INTERMIXED WITH THE REFINED COORDINATES. THEIR ABSENCE IS LIKELY TO BE MORE LIABLE TO CONFUSE THAN THEIR PRESENCE, ESPECIALLY WHEN CONSIDERED ALONGSIDE THE PUBLICATION.
RfactorNum. reflection% reflectionSelection details
Rfree0.146 4927 2 %RANDOM
Rwork0.112 ---
obs0.113 237810 95.4 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 23.33 Å2
Baniso -1Baniso -2Baniso -3
1--1.37 Å20 Å2-0.59 Å2
2--2.13 Å20 Å2
3----1.33 Å2
Refinement stepCycle: LAST / Resolution: 1.23→24.01 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5944 0 113 1046 7103
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.0216479
X-RAY DIFFRACTIONr_bond_other_d0.0020.025403
X-RAY DIFFRACTIONr_angle_refined_deg1.4731.9558849
X-RAY DIFFRACTIONr_angle_other_deg0.822312650
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.0955757
X-RAY DIFFRACTIONr_dihedral_angle_2_deg
X-RAY DIFFRACTIONr_dihedral_angle_3_deg
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.10.2959
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.027232
X-RAY DIFFRACTIONr_gen_planes_other0.0020.021340
X-RAY DIFFRACTIONr_nbd_refined0.20.21081
X-RAY DIFFRACTIONr_nbd_other0.2570.26308
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other0.0850.23706
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1370.2729
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined0.0810.215
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1730.239
X-RAY DIFFRACTIONr_symmetry_vdw_other0.3150.2241
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.160.280
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it6.97423780
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it8.79736164
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it12.19522693
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it14.6532670
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
LS refinement shellResolution: 1.23→1.26 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.26 353
Rwork0.229 17374

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