[English] 日本語
Yorodumi
- PDB-2c9q: Cu(I)Cu(II)-CopC at pH 7.5 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2c9q
TitleCu(I)Cu(II)-CopC at pH 7.5
ComponentsCOPPER RESISTANCE PROTEIN C
KeywordsELECTRON TRANSPORT(COPPER BINDING) / COPPER TRANSPORT / COPPER PROTEINS / COPPER DISSOCIATION CONSTANTS / METAL-BINDING / ELECTRON TRANSPORT
Function / homology
Function and homology information


copper ion transport / response to copper ion / periplasmic space / copper ion binding / plasma membrane
Similarity search - Function
Copper transport protein C/D / : / CopC domain / CopC domain / Immunoglobulin-like - #1220 / Copper resistance protein CopC/internalin, immunoglobulin-like / Immunoglobulin E-set / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
COPPER (II) ION / Copper resistance protein C
Similarity search - Component
Biological speciesPSEUDOMONAS SYRINGAE PV. TOMATO (bacteria)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.6 Å
AuthorsZhang, L. / Koay, M. / Maher, M.J. / Xiao, Z. / Wedd, A.G.
CitationJournal: J.Am.Chem.Soc. / Year: 2006
Title: Intermolecular Transfer of Copper Ions from the Copc Protein of Pseudomonas Syringae. Crystal Structures of Fully Loaded Cu(I)Cu(II) Forms.
Authors: Zhang, L. / Koay, M. / Maher, M.J. / Xiao, Z. / Wedd, A.G.
History
DepositionDec 14, 2005Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 3, 2006Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Dec 13, 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
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.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _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.pdbx_dist_value / _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_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

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: COPPER RESISTANCE PROTEIN C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)10,6743
Polymers10,5471
Non-polymers1272
Water1,49583
1
A: COPPER RESISTANCE PROTEIN C
hetero molecules

A: COPPER RESISTANCE PROTEIN C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,3486
Polymers21,0942
Non-polymers2544
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation8_555-y,-x,-z+1/21
MethodPQS
Unit cell
Length a, b, c (Å)55.781, 55.781, 60.261
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212
Components on special symmetry positions
IDModelComponents
11A-2049-

HOH

-
Components

#1: Protein COPPER RESISTANCE PROTEIN C / COPC


Mass: 10547.078 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) PSEUDOMONAS SYRINGAE PV. TOMATO (bacteria)
Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P12376
#2: Chemical ChemComp-CU / COPPER (II) ION


Mass: 63.546 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cu
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 83 / Source method: isolated from a natural source / Formula: H2O
Compound detailsFACILITATES COPPER RESISTANCE BY SEQUESTRATION OF COPPER IN THE PERIPLASM ALONG WITH THE COPPER- ...FACILITATES COPPER RESISTANCE BY SEQUESTRATION OF COPPER IN THE PERIPLASM ALONG WITH THE COPPER-BINDING PROTEIN COPA.

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 1.95 Å3/Da / Density % sol: 36.32 %
Crystal growpH: 7.5
Details: 2.0 M AMMONIUM SULFATE, 0.1 M SODIUM HEPES, PH 7.5, 2% (W/V) PEG 400

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5412
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Details: OSMIC MIRRORS
RadiationMonochromator: NI FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5412 Å / Relative weight: 1
ReflectionResolution: 1.6→50 Å / Num. obs: 13027 / % possible obs: 99.6 % / Observed criterion σ(I): 0 / Redundancy: 13.2 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 33
Reflection shellResolution: 1.6→1.66 Å / Redundancy: 11 % / Rmerge(I) obs: 0.32 / Mean I/σ(I) obs: 7.9 / % possible all: 100

-
Processing

Software
NameVersionClassification
REFMAC5refinement
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2C9P

2c9p


Resolution: 1.6→40 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.954 / SU B: 3.297 / SU ML: 0.059 / Cross valid method: THROUGHOUT / ESU R: 0.095 / ESU R Free: 0.097 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.225 633 4.9 %RANDOM
Rwork0.187 ---
obs0.189 12349 99.4 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 21.23 Å2
Baniso -1Baniso -2Baniso -3
1-0.58 Å20 Å20 Å2
2--0.58 Å20 Å2
3----1.15 Å2
Refinement stepCycle: LAST / Resolution: 1.6→40 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms738 0 2 83 823
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.022793
X-RAY DIFFRACTIONr_bond_other_d0.0010.02741
X-RAY DIFFRACTIONr_angle_refined_deg1.5391.9741084
X-RAY DIFFRACTIONr_angle_other_deg0.80831752
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.7055102
X-RAY DIFFRACTIONr_dihedral_angle_2_deg26.324.520
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.20715138
X-RAY DIFFRACTIONr_dihedral_angle_4_deg31.797151
X-RAY DIFFRACTIONr_chiral_restr0.0910.2139
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.02839
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02129
X-RAY DIFFRACTIONr_nbd_refined0.2060.2162
X-RAY DIFFRACTIONr_nbd_other0.1910.2705
X-RAY DIFFRACTIONr_nbtor_refined0.1710.2383
X-RAY DIFFRACTIONr_nbtor_other0.0850.2514
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1850.256
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1610.29
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2110.248
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2120.25
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it3.8162664
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it4.4683871
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it8.2024300
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it8.8416213
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→1.64 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.282 55
Rwork0.22 871
Refinement TLS params.Method: refined / Origin x: 9.173 Å / Origin y: -17.982 Å / Origin z: 2.529 Å
111213212223313233
T-0.026 Å2-0.0212 Å2-0.0242 Å2-0.0108 Å2-0.0151 Å2---0.0182 Å2
L0.8038 °2-0.3529 °2-1.0531 °2-0.6858 °20.8356 °2--1.6422 °2
S-0.0178 Å °0.2051 Å °0.008 Å °0.0819 Å °-0.0756 Å °0.0167 Å °0.1385 Å °-0.2865 Å °0.0935 Å °

+
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://pdbjlvh1.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