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- PDB-4ax3: Structure of three-domain heme-Cu nitrite reductase from Ralstoni... -

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Basic information

Entry
Database: PDB / ID: 4ax3
TitleStructure of three-domain heme-Cu nitrite reductase from Ralstonia pickettii at 1.6 A resolution
ComponentsCOPPER-CONTAINING NITRITE REDUCTASE
KeywordsOXIDOREDUCTASE / THREE-DOMAIN HEME-CU NITRITE REDUCTASE / ELECTRON TRANSFER / PROTON CHANNEL / DENITRIFICATION
Function / homology
Function and homology information


nitrite reductase (NO-forming) / nitrite reductase (NO-forming) activity / periplasmic space / electron transfer activity / copper ion binding / heme binding
Similarity search - Function
: / Cytochrome C oxidase, cbb3-type, subunit III / Nitrite reductase, copper-type / Cytochrome c / Cytochrome c-like domain / Cytochrome Bc1 Complex; Chain D, domain 2 / Multicopper oxidase, N-terminal / Multicopper oxidase / Cupredoxins - blue copper proteins / Cytochrome c family profile. ...: / Cytochrome C oxidase, cbb3-type, subunit III / Nitrite reductase, copper-type / Cytochrome c / Cytochrome c-like domain / Cytochrome Bc1 Complex; Chain D, domain 2 / Multicopper oxidase, N-terminal / Multicopper oxidase / Cupredoxins - blue copper proteins / Cytochrome c family profile. / Cytochrome c-like domain / Cytochrome c-like domain superfamily / Cupredoxin / Immunoglobulin-like / Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
COPPER (II) ION / HEME C / Copper-containing nitrite reductase / :
Similarity search - Component
Biological speciesRALSTONIA PICKETTII (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.6 Å
AuthorsAntonyuk, S.V. / Cong, H. / Eady, R.R. / Hasnain, S.S.
CitationJournal: Nature / Year: 2013
Title: Structures of protein-protein complexes involved in electron transfer.
Authors: Antonyuk, S.V. / Han, C. / Eady, R.R. / Hasnain, S.S.
History
DepositionJun 7, 2012Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 27, 2013Provider: repository / Type: Initial release
Revision 1.1Apr 17, 2013Group: Database references
Revision 2.0Jan 23, 2019Group: 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 / citation / entity / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_conn_angle / pdbx_struct_special_symmetry / struct_conn
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_atom_id / _atom_site.auth_comp_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.type_symbol / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.name / _chem_comp.pdbx_synonyms / _citation.journal_id_ISSN / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _entity.formula_weight / _entity.pdbx_description / _pdbx_entity_nonpoly.comp_id / _pdbx_entity_nonpoly.name / _pdbx_nonpoly_scheme.mon_id / _pdbx_nonpoly_scheme.pdb_mon_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_label_comp_id
Revision 2.1Dec 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 / pdbx_struct_conn_angle / struct_conn / struct_conn_type / struct_site
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 / _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 / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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.ptnr1_symmetry / _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_label_seq_id / _struct_conn.ptnr2_symmetry / _struct_conn_type.id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: COPPER-CONTAINING NITRITE REDUCTASE
B: COPPER-CONTAINING NITRITE REDUCTASE
C: COPPER-CONTAINING NITRITE REDUCTASE
D: COPPER-CONTAINING NITRITE REDUCTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)202,77616
Polymers199,7944
Non-polymers2,98212
Water44,4972470
1
B: COPPER-CONTAINING NITRITE REDUCTASE
hetero molecules

B: COPPER-CONTAINING NITRITE REDUCTASE
hetero molecules

B: COPPER-CONTAINING NITRITE REDUCTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)152,08212
Polymers149,8463
Non-polymers2,2379
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation11_466y-1/2,-z+3/2,-x+11
crystal symmetry operation8_656-z+1,x+1/2,-y+3/21
Buried area18040 Å2
ΔGint-215.4 kcal/mol
Surface area44650 Å2
MethodPISA
2
A: COPPER-CONTAINING NITRITE REDUCTASE
hetero molecules

A: COPPER-CONTAINING NITRITE REDUCTASE
hetero molecules

A: COPPER-CONTAINING NITRITE REDUCTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)152,08212
Polymers149,8463
Non-polymers2,2379
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation10_655-y+1,z+1/2,-x+1/21
crystal symmetry operation7_564-z+1/2,-x+1,y-1/21
Buried area18270 Å2
ΔGint-209.3 kcal/mol
Surface area45720 Å2
MethodPISA
3
C: COPPER-CONTAINING NITRITE REDUCTASE
hetero molecules

C: COPPER-CONTAINING NITRITE REDUCTASE
hetero molecules

C: COPPER-CONTAINING NITRITE REDUCTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)152,08212
Polymers149,8463
Non-polymers2,2379
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation12_565-y+1/2,-z+1,x+1/21
crystal symmetry operation6_456z-1/2,-x+1/2,-y+11
Buried area18150 Å2
ΔGint-205.1 kcal/mol
Surface area44360 Å2
MethodPISA
4
D: COPPER-CONTAINING NITRITE REDUCTASE
hetero molecules

D: COPPER-CONTAINING NITRITE REDUCTASE
hetero molecules

D: COPPER-CONTAINING NITRITE REDUCTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)152,08212
Polymers149,8463
Non-polymers2,2379
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation9_555y,z,x1
crystal symmetry operation5_555z,x,y1
Buried area18450 Å2
ΔGint-195.3 kcal/mol
Surface area44700 Å2
MethodPISA
Unit cell
Length a, b, c (Å)185.812, 185.812, 185.812
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number198
Space group name H-MP213
Components on special symmetry positions
IDModelComponents
11A-2217-

HOH

21A-2218-

HOH

31A-2236-

HOH

41A-2249-

HOH

51A-2252-

HOH

61A-2254-

HOH

71A-2381-

HOH

81B-2190-

HOH

91B-2191-

HOH

101B-2192-

HOH

111B-2210-

HOH

121B-2223-

HOH

131B-2225-

HOH

141B-2228-

HOH

151C-2201-

HOH

161C-2202-

HOH

171C-2222-

HOH

181C-2237-

HOH

191C-2238-

HOH

201C-2241-

HOH

211C-2393-

HOH

221D-2147-

HOH

231D-2148-

HOH

241D-2162-

HOH

251D-2173-

HOH

261D-2174-

HOH

271D-2285-

HOH

281D-2352-

HOH

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Components

#1: Protein
COPPER-CONTAINING NITRITE REDUCTASE


Mass: 49948.516 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) RALSTONIA PICKETTII (bacteria) / Strain: 12J / Description: GENBANK ACCESSION NUMBER. NC_010678 / Plasmid: PET26B-RPNIR / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: E2STD2, UniProt: B2UHR8*PLUS, nitrite reductase (NO-forming)
#2: Chemical
ChemComp-CU / COPPER (II) ION


Mass: 63.546 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Cu
#3: Chemical
ChemComp-HEC / HEME C


Mass: 618.503 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C34H34FeN4O4
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 2470 / Source method: isolated from a natural source / Formula: H2O

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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: 2.4 Å3/Da / Density % sol: 49.5 % / Description: NONE
Crystal growpH: 6.5 / Details: PEG, SODIUM CITRITE, pH 6.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 1 / Wavelength: 0.98
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Mar 31, 2012 / Details: MIRRORS
RadiationMonochromator: SI111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 1.6→25 Å / Num. obs: 278689 / % possible obs: 99.9 % / Redundancy: 8 % / Biso Wilson estimate: 20.7 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 25
Reflection shellResolution: 1.6→1.66 Å / Redundancy: 6.2 % / Rmerge(I) obs: 0.8 / Mean I/σ(I) obs: 2 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.5.0109refinement
HKL-2000data reduction
HKL-2000data scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4AWW

4aww
PDB Unreleased entry


Resolution: 1.6→25 Å / Cor.coef. Fo:Fc: 0.974 / Cor.coef. Fo:Fc free: 0.964 / SU B: 1.585 / SU ML: 0.055 / Cross valid method: THROUGHOUT / ESU R: 0.078 / ESU R Free: 0.08 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.19411 14041 5 %RANDOM
Rwork0.16296 ---
obs0.16453 264055 99.82 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 17.703 Å2
Refinement stepCycle: LAST / Resolution: 1.6→25 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13728 0 180 2470 16378
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.02214757
X-RAY DIFFRACTIONr_bond_other_d0.0010.029898
X-RAY DIFFRACTIONr_angle_refined_deg1.5321.99720217
X-RAY DIFFRACTIONr_angle_other_deg0.92324316
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.54151958
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.19524.522628
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.653152340
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.5291568
X-RAY DIFFRACTIONr_chiral_restr0.0930.22183
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.02116808
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022844
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_it0.7991.59267
X-RAY DIFFRACTIONr_mcbond_other0.2431.53796
X-RAY DIFFRACTIONr_mcangle_it1.356215005
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.1635490
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it3.3584.55143
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: 1.6→1.641 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.322 1037 -
Rwork0.292 19412 -
obs--99.93 %

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