[English] 日本語
Yorodumi
- PDB-2qzy: The structure of chicken mitochondrial PEPCK in complex with PEP -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2qzy
TitleThe structure of chicken mitochondrial PEPCK in complex with PEP
ComponentsPhosphoenolpyruvate carboxykinase [GTP]
KeywordsLYASE / pepck / kinase / Decarboxylase / Gluconeogenesis / GTP-binding / Manganese / Mitochondrion / Nucleotide-binding / Transit peptide
Function / homology
Function and homology information


eggshell formation / lactate oxidation / egg-laying behavior / regulation of viral process / Gluconeogenesis / glycerol biosynthetic process from pyruvate / phosphoenolpyruvate carboxykinase (GTP) / phosphoenolpyruvate carboxykinase (GTP) activity / propionate catabolic process / embryonic organ morphogenesis ...eggshell formation / lactate oxidation / egg-laying behavior / regulation of viral process / Gluconeogenesis / glycerol biosynthetic process from pyruvate / phosphoenolpyruvate carboxykinase (GTP) / phosphoenolpyruvate carboxykinase (GTP) activity / propionate catabolic process / embryonic organ morphogenesis / vitellogenesis / lactate metabolic process / glycerol catabolic process / hepatocyte differentiation / pyruvate metabolic process / cellular response to ethanol / glucose catabolic process to lactate via pyruvate / embryo development ending in birth or egg hatching / regulation of gluconeogenesis / response to starvation / response to cAMP / cellular response to dexamethasone stimulus / gluconeogenesis / cellular response to glucose stimulus / cellular response to insulin stimulus / manganese ion binding / mitochondrial matrix / GTP binding / cytosol
Similarity search - Function
Phosphoenolpyruvate carboxykinase, GTP-utilising / Phosphoenolpyruvate carboxykinase, GTP-utilising, conserved site / Phosphoenolpyruvate carboxykinase, C-terminal P-loop domain / Phosphoenolpyruvate carboxykinase, GTP-utilising, N-terminal / Phosphoenolpyruvate carboxykinase C-terminal P-loop domain / Phosphoenolpyruvate carboxykinase N-terminal domain / Phosphoenolpyruvate carboxykinase (GTP) signature. / Phosphoenolpyruvate Carboxykinase; domain 2 / Phosphoenolpyruvate Carboxykinase, domain 2 / Phosphoenolpyruvate Carboxykinase; domain 1 ...Phosphoenolpyruvate carboxykinase, GTP-utilising / Phosphoenolpyruvate carboxykinase, GTP-utilising, conserved site / Phosphoenolpyruvate carboxykinase, C-terminal P-loop domain / Phosphoenolpyruvate carboxykinase, GTP-utilising, N-terminal / Phosphoenolpyruvate carboxykinase C-terminal P-loop domain / Phosphoenolpyruvate carboxykinase N-terminal domain / Phosphoenolpyruvate carboxykinase (GTP) signature. / Phosphoenolpyruvate Carboxykinase; domain 2 / Phosphoenolpyruvate Carboxykinase, domain 2 / Phosphoenolpyruvate Carboxykinase; domain 1 / Phosphoenolpyruvate Carboxykinase, domain 1 / Phosphoenolpyruvate Carboxykinase; domain 3 - #20 / Phosphoenolpyruvate carboxykinase, C-terminal / Phosphoenolpyruvate carboxykinase, N-terminal / Phosphoenolpyruvate Carboxykinase; domain 3 / Beta Complex / Alpha-Beta Complex / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
octanoyl-sucrose, esterificated at glucose C6 / : / PHOSPHOENOLPYRUVATE / Phosphoenolpyruvate carboxykinase [GTP], mitochondrial
Similarity search - Component
Biological speciesGallus gallus (chicken)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.9 Å
AuthorsHolyoak, T. / Sullivan, S.M. / Nowak, T.
CitationJournal: Biochemistry / Year: 2006
Title: Structural Insights into the Mechanism of PEPCK Catalysis
Authors: Holyoak, T. / Sullivan, S.M. / Nowak, T.
History
DepositionAug 17, 2007Deposition site: RCSB / Processing site: RCSB
SupersessionSep 4, 2007ID: 2FAG
Revision 1.0Sep 4, 2007Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Oct 25, 2017Group: Refinement description / Category: software
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations / Non-polymer description / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / entity_name_com / 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_molecule_features / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / struct_asym / struct_conn / struct_conn_type / struct_ref_seq_dif
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 / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.pdbx_synonyms / _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.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _struct_asym.entity_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Aug 30, 2023Group: Data collection / Database references ...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
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Remark 999SEQUENCE THE CHANGES IN THE PROTEIN SEQUENCE REPRESENT ERRORS IN THE ORIGINAL PUBLISHED SEQUENCE. ...SEQUENCE THE CHANGES IN THE PROTEIN SEQUENCE REPRESENT ERRORS IN THE ORIGINAL PUBLISHED SEQUENCE. THESE CHANGES WERE VERIFIED BY RESEQUENCING OF THE GENE AND MASS SPECTROMETRY ANALYSIS.

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Phosphoenolpyruvate carboxykinase [GTP]
B: Phosphoenolpyruvate carboxykinase [GTP]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)135,9378
Polymers134,7842
Non-polymers1,1536
Water17,943996
1
A: Phosphoenolpyruvate carboxykinase [GTP]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)67,8534
Polymers67,3921
Non-polymers4613
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Phosphoenolpyruvate carboxykinase [GTP]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)68,0834
Polymers67,3921
Non-polymers6913
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)110.349, 48.023, 126.317
Angle α, β, γ (deg.)90.00, 111.39, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

-
Protein / Sugars , 2 types, 3 molecules AB

#1: Protein Phosphoenolpyruvate carboxykinase [GTP] / Phosphoenolpyruvate carboxylase / PEPCK-M


Mass: 67391.883 Da / Num. of mol.: 2 / Fragment: mature mitochondrial protein, UNP residues 34-640 / Source method: isolated from a natural source / Details: mature mitochondrial protein / Source: (natural) Gallus gallus (chicken)
References: UniProt: P21642, phosphoenolpyruvate carboxykinase (GTP)
#2: Polysaccharide beta-D-fructofuranose-(2-1)-6-O-octanoyl-alpha-D-glucopyranose / octanoyl-sucrose / esterificated at glucose C6


Type: oligosaccharide, Oligosaccharide / Class: Substrate analog / Mass: 468.493 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: oligosaccharide with reducing-end-to-reducing-end glycosidic bond
References: octanoyl-sucrose, esterificated at glucose C6
DescriptorTypeProgram
WURCS=2.0/2,2,1/[ha122h-2b_2-5][a2122h-1a_1-5_6*OCCCCCCCC/3=O]/1-2/a2-b1WURCSPDB2Glycan 1.1.0
[][b-D-Fruf]{[(2+1)][a-D-Glcp]{}}LINUCSPDB-CARE

-
Non-polymers , 4 types, 1001 molecules

#3: Chemical ChemComp-EPE / 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / HEPES / HEPES


Mass: 238.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C8H18N2O4S / Comment: pH buffer*YM
#4: Chemical ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mn
#5: Chemical ChemComp-PEP / PHOSPHOENOLPYRUVATE / Phosphoenolpyruvic acid


Mass: 168.042 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H5O6P
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 996 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.31 Å3/Da / Density % sol: 46.8 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.4
Details: 19% PEG6000, 0.1M HEPES pH 7.4, N-OCTANOYL SUCROSE, hanging drop vapor diffusion, temperature 293K, VAPOR DIFFUSION, HANGING DROP

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL11-1 / Wavelength: 0.9 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: May 15, 2004
RadiationProtocol: SINGLE WAVELENGTH / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9 Å / Relative weight: 1
ReflectionResolution: 1.9→50 Å / Num. obs: 95642 / % possible obs: 97.9 % / Redundancy: 4.9 % / Rmerge(I) obs: 0.117 / Χ2: 1.089 / Net I/σ(I): 7.6
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2Diffraction-ID% possible all
1.9-1.974.50.59692460.914195.8
1.97-2.054.50.45192690.976196
2.05-2.144.50.35493941.047196.3
2.14-2.254.60.27893811.099196.8
2.25-2.394.70.23494751.092197.3
2.39-2.584.80.1995581.122198.6
2.58-2.845.10.14196911.13199.4
2.84-3.255.40.1197851.095199.9
3.25-4.095.40.07498161.158199.8
4.09-505.50.061100271.184199.3

-
Phasing

PhasingMethod: molecular replacement

-
Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
REFMACrefinement
PDB_EXTRACT3data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2FAF
Resolution: 1.9→35.09 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.943 / SU B: 5.777 / SU ML: 0.09 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.146 / ESU R Free: 0.133 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.2 4789 5 %RANDOM
Rwork0.161 ---
obs0.163 95631 97.8 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 20.794 Å2
Baniso -1Baniso -2Baniso -3
1--0.03 Å20 Å2-0.02 Å2
2--0.01 Å20 Å2
3---0.01 Å2
Refinement stepCycle: LAST / Resolution: 1.9→35.09 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9315 0 69 996 10380
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.0229811
X-RAY DIFFRACTIONr_angle_refined_deg1.3241.97113380
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.7851231
X-RAY DIFFRACTIONr_dihedral_angle_2_deg28.75222.173451
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.993151523
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.65615108
X-RAY DIFFRACTIONr_chiral_restr0.0810.21376
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.027758
X-RAY DIFFRACTIONr_nbd_refined0.1920.24732
X-RAY DIFFRACTIONr_nbtor_refined0.3080.26635
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1310.2976
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.230.2100
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2080.238
X-RAY DIFFRACTIONr_mcbond_it0.5161.56188
X-RAY DIFFRACTIONr_mcangle_it0.76829729
X-RAY DIFFRACTIONr_scbond_it1.39934168
X-RAY DIFFRACTIONr_scangle_it2.214.53630
LS refinement shellResolution: 1.9→1.95 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.24 326 -
Rwork0.207 6330 -
all-6656 -
obs--93.77 %
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)
11.5477-0.51920.52921.8071-0.88840.84770.00730.01810.0121-0.06290.03490.0836-0.0493-0.0776-0.0422-0.08870.01170.0456-0.12150.0248-0.136-16.925-40.58474.184
21.002-0.05890.5270.36420.02723.0228-0.06290.06820.01160.0375-0.02350.0054-0.21410.03190.0865-0.06490.0080.0213-0.17980.0099-0.1228-6.459-44.72974.851
31.7223-0.4488-0.12673.86682.17392.52690.09240.098-0.0313-0.25690.062-0.3199-0.0621-0.1504-0.1544-0.0685-0.02140.0355-0.0842-0.0209-0.095-9.421-53.22648.515
42.61860.6851.08131.7463.91979.58240.0829-0.0175-0.18720.1522-0.01260.09990.20660.0171-0.0703-0.10870.02250.0506-0.14510.0286-0.1305-23.361-42.78575.9
51.9461-0.4204-0.07461.0764-0.10531.8503-0.0042-0.01010.01440.08170.0427-0.01010.0872-0.0056-0.0385-0.08220.00940.0085-0.2045-0.0066-0.1528-8.285-40.23677.651
61.9834-0.5262-0.35351.466-0.95463.45610.07510.1722-0.07150.05120.01570.0964-0.029-0.2037-0.0909-0.11530.0350.0155-0.1445-0.0166-0.1497-17.047-43.13471.71
72.22130.8536-1.15481.725-0.08732.5464-0.07310.0412-0.02220.02470.079-0.02410.007-0.0141-0.0058-0.1230.00570.0169-0.16540.0054-0.127-11.963-46.88367.575
818.9028-2.3603-5.914512.9368-7.71516.731-0.1658-0.44720.2177-0.023-0.54980.103-0.3060.22450.7156-0.1203-0.02450.0118-0.1599-0.0064-0.1572-1.242-39.88355.573
95.6488-0.10181.321.40780.5891.9724-0.11820.02170.053-0.04110.0462-0.0816-0.01180.03190.072-0.1185-0.02110.0459-0.1516-0.0007-0.15438.163-42.38759.682
103.8696-0.6230.14741.02850.18522.39950.0350.07460.1817-0.031-0.06140.0505-0.1777-0.37330.0264-0.07140.00990.0254-0.0952-0.0073-0.0994-0.546-37.22562.044
114.4661.7493-8.33332.5298-3.834122.9096-0.0088-0.0280.00120.0325-0.0837-0.1637-0.0431-0.17210.0925-0.1314-0.00570.0049-0.16670.0063-0.12964.366-39.17869.945
122.24220.7553-0.62371.6685-0.2571.3263-0.07230.10770.0779-0.00760.08910.09250.001-0.0039-0.0168-0.05510.01730.0063-0.18180.022-0.1261-4.778-49.48483.491
132.05991.0079-0.65122.1575-1.18942.1468-0.0360.09530.03820.00110.10450.03530.05490.0655-0.0684-0.090.03490.0087-0.1685-0.0148-0.13553.016-47.0777.403
141.2067-0.6161-0.19471.08780.79011.28170.04890.01290.0112-0.1418-0.036-0.1717-0.1205-0.002-0.013-0.10890.00160.0488-0.1560.0402-0.1111.96-45.1753.252
155.2604-3.0738-3.01335.33074.17075.11050.1229-0.0922-0.025-0.064-0.27930.0543-0.1496-0.34840.1564-0.10660.00480.0089-0.121-0.0072-0.1618-1.664-47.60358.491
165.9150.6418-1.15510.84370.76632.4103-0.0207-0.3142-0.2153-0.0713-0.14820.03730.0198-0.07050.1689-0.08440.0130.0185-0.13730.0146-0.1309-0.963-48.52853.207
172.7580.24540.7476.5937-0.98243.1948-0.05690.01740.0093-0.44830.10820.10990.0760.0069-0.0513-0.11680.02680.0423-0.14270.0268-0.080416.515-53.12755.085
183.3780.3068-0.833.4571.11133.631-0.21050.7482-0.068-0.9478-0.24680.1471-0.114-0.61720.45730.15620.01340.01010.1166-0.0589-0.015512.965-56.00339.922
196.0373-0.48973.31481.17110.33223.2634-0.104-0.0188-0.0102-0.0264-0.0643-0.07350.1860.05550.1683-0.028-0.01930.075-0.14040.0345-0.026310.861-63.94348.386
202.9582-0.8748-0.67832.3147-0.40371.6559-0.0180.1149-0.0454-0.0507-0.0663-0.06850.0009-0.06390.0843-0.0734-0.03340.038-0.1429-0.0064-0.12472.768-56.02246.11
214.9198-1.31740.30243.2443-0.30315.4266-0.0203-0.13020.3316-0.09310.19030.07270.1417-0.7368-0.170.0737-0.0754-0.06070.07630.0155-0.006516.976-62.304-12.772
221.84692.4076-1.63226.2042-3.03734.08610.0297-0.04170.0689-0.17030.026-0.1224-0.07060.3217-0.05570.018-0.0030.0632-0.04120.0045-0.090840.221-52.566-18.805
231.3256-0.1759-0.56011.4008-0.30793.40380.12590.05840.1448-0.0077-0.02650.0042-0.1804-0.0239-0.0994-0.01330.00820.0212-0.09890.0405-0.107631.433-49.074-5.304
242.7574-0.5855-0.10411.20690.11358.36980.07880.24640.1322-0.08080.02460.1432-0.131-0.1172-0.1034-0.05240.06660.02550.11820.1154-0.055915.059-51.8990.921
251.1930.06230.14130.7548-0.09953.053-0.06410.00910.0252-0.07870.06330.00960.11440.03250.0008-0.00870.00050.0191-0.10290.031-0.115630.395-61.089-6.4
262.223-0.3424-0.00734.3561-2.56036.4922-0.00270.13830.0387-0.13560.12240.13870.0993-0.3648-0.1197-0.0459-0.035-0.0265-0.03070.0254-0.114421.039-60.146-12.317
273.83650.5165-2.58472.3729-1.99575.42530.0245-0.17460.1074-0.06580.02210.0073-0.04190.1275-0.0466-0.05170.01490.0007-0.070.0126-0.142226.229-52.972-5.491
280.51970.4582-1.14391.1199-2.25345.37910.0563-0.0441-0.0632-0.0107-0.05580.0925-0.1331-0.1038-0.00050.00320.0432-0.0205-0.03240.0333-0.088223.498-52.926-3.06
297.7772-4.08583.7452.5303-1.3424.40310.32450.1615-0.4223-0.0409-0.10740.16070.15290.0552-0.217-0.05380.01040.0273-0.05560.0594-0.105431.239-61.26818.949
3013.5462-2.85052.72773.1905-0.84820.5783-0.1904-0.4947-0.15320.32260.02640.0531-0.50930.04810.1640.0692-0.02320.11570.2210.06260.08141.911-55.78322.149
315.8195-0.3442.70441.1386-0.69266.0125-0.05940.67750.1024-0.01820.10880.00820.0435-0.0658-0.0494-0.04730.03230.0247-0.03250.0536-0.109627.967-60.98710.601
321.67390.7634-0.82952.0978-1.97553.5758-0.06870.007-0.0314-0.08680.23710.12710.2594-0.3011-0.16840.0180.02110.0119-0.04420.0595-0.102627.188-63.6127.489
334.89510.48271.29714.6312-2.65275.1950.26450.1351-0.4632-0.4410.22190.47750.7036-0.3894-0.48640.0527-0.0342-0.0693-0.01080.0191-0.021931.08-57.942-6.503
341.3829-0.77970.26843.0775-1.48093.6750.0416-0.09370.0687-0.21410.08070.0733-0.1023-0.0025-0.1223-0.0443-0.00220.0314-0.06060.0017-0.098233.992-52.2610.892
351.66610.95970.54264.571.57382.82310.17240.08460.10860.2756-0.0693-0.05210.15270.0665-0.1031-0.0788-0.01540.033-0.05590.0868-0.108732.454-57.30826.684
365.252-0.43631.32273.54120.04125.59110.0554-0.1426-0.13940.1957-0.1185-0.13070.0569-0.02170.0631-0.0621-0.01220.0596-0.11850.0199-0.102223.834-55.55733.159
371.89250.3476-0.65280.9461-0.38073.58660.06640.0667-0.05720.0291-0.06450.0282-0.112-0.1047-0.0019-0.05130.01770.05-0.07520.0425-0.091922.477-54.33519.55
382.4901-0.8357-0.54152.7784-0.22272.5146-0.05150.0735-0.06650.10850.03010.24690.1064-0.04190.0214-0.0458-0.02150.0194-0.09630.0442-0.079429.446-57.07232.222
391.7425-0.3139-0.45191.31981.66044.48190.1008-0.46390.26560.38380.2708-0.20470.24250.5899-0.37160.0980.02580.02450.0798-0.02960.006725.589-44.87948.081
4018.0888-2.2509-8.125513.7216-5.71347.0141-0.45341.5789-1.3049-1.15470.00170.24190.666-0.57540.45170.0516-0.02480.08060.0023-0.09020.033518.26-47.75334.715
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1X-RAY DIFFRACTION1AA34 - 801 - 47
2X-RAY DIFFRACTION2AA81 - 11748 - 84
3X-RAY DIFFRACTION3AA118 - 14085 - 107
4X-RAY DIFFRACTION4AA141 - 157108 - 124
5X-RAY DIFFRACTION5AA158 - 196125 - 163
6X-RAY DIFFRACTION6AA197 - 232164 - 199
7X-RAY DIFFRACTION7AA233 - 270200 - 237
8X-RAY DIFFRACTION8AA271 - 276238 - 243
9X-RAY DIFFRACTION9AA277 - 308244 - 275
10X-RAY DIFFRACTION10AA309 - 334276 - 301
11X-RAY DIFFRACTION11AA335 - 351302 - 318
12X-RAY DIFFRACTION12AA352 - 388319 - 355
13X-RAY DIFFRACTION13AA389 - 443356 - 410
14X-RAY DIFFRACTION14AA444 - 473411 - 440
15X-RAY DIFFRACTION15AA474 - 505441 - 472
16X-RAY DIFFRACTION16AA506 - 528473 - 495
17X-RAY DIFFRACTION17AA529 - 563496 - 530
18X-RAY DIFFRACTION18AA564 - 594531 - 561
19X-RAY DIFFRACTION19AA595 - 613562 - 580
20X-RAY DIFFRACTION20AA614 - 641581 - 608
21X-RAY DIFFRACTION21BB34 - 611 - 28
22X-RAY DIFFRACTION22BB62 - 8329 - 50
23X-RAY DIFFRACTION23BB84 - 10851 - 75
24X-RAY DIFFRACTION24BB109 - 14776 - 114
25X-RAY DIFFRACTION25BB148 - 199115 - 166
26X-RAY DIFFRACTION26BB200 - 223167 - 190
27X-RAY DIFFRACTION27BB224 - 250191 - 217
28X-RAY DIFFRACTION28BB251 - 281218 - 248
29X-RAY DIFFRACTION29BB282 - 306249 - 273
30X-RAY DIFFRACTION30BB307 - 319274 - 286
31X-RAY DIFFRACTION31BB320 - 339287 - 306
32X-RAY DIFFRACTION32BB340 - 371307 - 338
33X-RAY DIFFRACTION33BB372 - 418339 - 385
34X-RAY DIFFRACTION34BB419 - 443386 - 410
35X-RAY DIFFRACTION35BB444 - 463411 - 430
36X-RAY DIFFRACTION36BB464 - 495431 - 462
37X-RAY DIFFRACTION37BB496 - 529463 - 496
38X-RAY DIFFRACTION38BB530 - 601497 - 568
39X-RAY DIFFRACTION39BB602 - 636569 - 603
40X-RAY DIFFRACTION40BB637 - 641604 - 608

+
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