[English] 日本語
Yorodumi
- PDB-3hd6: Crystal Structure of the Human Rhesus Glycoprotein RhCG -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3hd6
TitleCrystal Structure of the Human Rhesus Glycoprotein RhCG
ComponentsAmmonium transporter Rh type C
KeywordsMEMBRANE PROTEIN / TRANSPORT PROTEIN / ammonia / channel / rhesus / glycoprotein / transporter / membrane / Structural Genomics / PSI-2 / Protein Structure Initiative / Center for Structures of Membrane Proteins / CSMP / Ammonia transport / Cell membrane / Transmembrane / Transport
Function / homology
Function and homology information


amine transport / Rhesus glycoproteins mediate ammonium transport / transepithelial ammonium transport / carbon dioxide transmembrane transporter activity / ammonium homeostasis / ammonium transmembrane transport / intracellular monoatomic ion homeostasis / ammonium channel activity / regulation of pH / ankyrin binding ...amine transport / Rhesus glycoproteins mediate ammonium transport / transepithelial ammonium transport / carbon dioxide transmembrane transporter activity / ammonium homeostasis / ammonium transmembrane transport / intracellular monoatomic ion homeostasis / ammonium channel activity / regulation of pH / ankyrin binding / homeostatic process / epithelial cell differentiation / basolateral plasma membrane / cytoplasmic vesicle / apical plasma membrane / extracellular exosome / identical protein binding / plasma membrane
Similarity search - Function
Blood group Rhesus C/E/D polypeptide / Ammonium transporter fold / Ammonium transporter AmtB like domains / Ammonium transporter AmtB-like domain / Ammonium Transporter Family / Ammonium/urea transporter / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Ammonium transporter Rh type C
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å
AuthorsGruswitz, F. / Chaudhary, S. / Ho, J.D. / Pezeshki, B. / Ho, C.-M. / Stroud, R.M. / Center for Structures of Membrane Proteins (CSMP)
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2010
Title: Function of human Rh based on structure of RhCG at 2.1 A.
Authors: Gruswitz, F. / Chaudhary, S. / Ho, J.D. / Schlessinger, A. / Pezeshki, B. / Ho, C.M. / Sali, A. / Westhoff, C.M. / Stroud, R.M.
History
DepositionMay 6, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 1, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Jan 24, 2018Group: Structure summary / Category: audit_author / Item: _audit_author.name
Revision 1.3Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_site / struct_site_gen
Item: _chem_comp.mon_nstd_flag / _chem_comp.name ..._chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.4Mar 31, 2021Group: Source and taxonomy / Structure summary / Category: chem_comp / entity_src_gen
Item: _chem_comp.pdbx_synonyms / _entity_src_gen.pdbx_host_org_cell_line / _entity_src_gen.pdbx_host_org_strain
Revision 1.5Sep 6, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Ammonium transporter Rh type C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)54,4712
Polymers54,1791
Non-polymers2921
Water2,090116
1
A: Ammonium transporter Rh type C
hetero molecules

A: Ammonium transporter Rh type C
hetero molecules

A: Ammonium transporter Rh type C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)163,4136
Polymers162,5363
Non-polymers8773
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_665-y+1,x-y+1,z1
crystal symmetry operation3_565-x+y,-x+1,z1
Buried area18610 Å2
ΔGint-150 kcal/mol
Surface area37580 Å2
MethodPISA
Unit cell
Length a, b, c (Å)99.830, 99.830, 101.076
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number173
Space group name H-MP63
Components on special symmetry positions
IDModelComponents
11A-593-

HOH

21A-594-

HOH

31A-598-

HOH

DetailsThe biological assembly is a trimer generated from the monomer in the asymmetric unit by the threefold symmetry axis

-
Components

#1: Protein Ammonium transporter Rh type C / Rhesus blood group family type C glycoprotein / Rh family type C glycoprotein / Rh type C ...Rhesus blood group family type C glycoprotein / Rh family type C glycoprotein / Rh type C glycoprotein / Tumor-related protein DRC2 / Rh glycoprotein kidney


Mass: 54178.586 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: suspension growth of human endothelial kidney cells
Source: (gene. exp.) Homo sapiens (human) / Gene: C15orf6, CDRC2, PDRC2, RHCG, RHGK / Plasmid details: stable transfection / Plasmid: pACMV-tetO-Rho / Cell line (production host): HEK293S / Production host: Homo sapiens (human) / References: UniProt: Q9UBD6
#2: Sugar ChemComp-BOG / octyl beta-D-glucopyranoside / Beta-Octylglucoside / octyl beta-D-glucoside / octyl D-glucoside / octyl glucoside


Type: D-saccharide / Mass: 292.369 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Formula: C14H28O6 / Comment: detergent*YM
IdentifierTypeProgram
b-octylglucosideIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 116 / 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: 2.68 Å3/Da / Density % sol: 54.17 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: 0.1M Tris pH 8.5 (at 293K), 40% PEG 200 + 20mM Tris pH 7.4 (at 293K), 100mM NaCl, 40mM BOG, VAPOR DIFFUSION, HANGING DROP, temperature 277K

-
Data collection

DiffractionMean temperature: 80 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 1.11587 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Dec 8, 2008
RadiationMonochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.11587 Å / Relative weight: 1
ReflectionResolution: 2.1→86.39 Å / Num. all: 33464 / Num. obs: 33449 / % possible obs: 99.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 2 / Redundancy: 10.6 % / Rmerge(I) obs: 0.077 / Rsym value: 0.089 / Net I/σ(I): 39.7
Reflection shellResolution: 2.1→2.18 Å / Redundancy: 8.6 % / Rmerge(I) obs: 0.589 / Mean I/σ(I) obs: 3.4 / Rsym value: 0.637 / % possible all: 95.8

-
Processing

Software
NameVersionClassification
ADSCQuantumdata collection
PHASERphasing
REFMAC5.4.0067refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3B9W
Resolution: 2.1→86.39 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.941 / SU B: 6.507 / SU ML: 0.079 / TLS residual ADP flag: LIKELY RESIDUAL / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / ESU R: 0.152 / ESU R Free: 0.134 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.19505 1695 5.1 %RANDOM
Rwork0.16837 ---
obs0.16973 31746 99.68 %-
all-33464 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 24.109 Å2
Baniso -1Baniso -2Baniso -3
1-0.69 Å20.34 Å20 Å2
2--0.69 Å20 Å2
3----1.03 Å2
Refinement stepCycle: LAST / Resolution: 2.1→86.39 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3163 0 20 116 3299
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0090.0223265
X-RAY DIFFRACTIONr_bond_other_d0.0010.022140
X-RAY DIFFRACTIONr_angle_refined_deg1.0181.9414432
X-RAY DIFFRACTIONr_angle_other_deg0.8735191
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.1335400
X-RAY DIFFRACTIONr_dihedral_angle_2_deg38.15923.188138
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.60215511
X-RAY DIFFRACTIONr_dihedral_angle_4_deg9.6761514
X-RAY DIFFRACTIONr_chiral_restr0.0660.2503
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.023608
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02733
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_it0.4291.51985
X-RAY DIFFRACTIONr_mcbond_other0.0951.5832
X-RAY DIFFRACTIONr_mcangle_it0.7923185
X-RAY DIFFRACTIONr_scbond_it1.20431280
X-RAY DIFFRACTIONr_scangle_it1.8814.51247
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.097→2.152 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.209 136 -
Rwork0.198 2258 -
obs--95.8 %
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)
10.95850.1586-0.4560.9861-0.57044.8534-0.0598-0.0425-0.3746-0.0573-0.0755-0.36730.49840.63090.13530.16170.10960.00140.2276-0.00040.255423.29938.80439.325
210.266-4.17962.342621.8641-3.427723.25430.0449-1.1515-0.73161.58790.09710.1090.2039-0.0002-0.1420.4624-0.08960.0240.43840.01960.09786.65151.22963.678
30.62450.1699-0.09151.4437-0.54570.78590.02280.0213-0.03590.0216-0.0257-0.13730.07130.15570.00290.12450.0170.00190.1734-0.00950.073213.553.09940.231
44.52415.7775-5.702714.2624-10.308516.16090.1175-0.15870.26940.8062-0.3678-0.40750.14330.38690.25030.27820.0538-0.10340.3786-0.00070.209326.97146.56960.63
52.8575-5.41882.891211.1528-7.67839.0003-0.3363-0.20840.07280.84650.2978-0.2203-0.53640.07330.03850.26950.0019-0.14980.2377-0.00650.145919.40647.16559.011
60.6495-0.05370.3311.4186-0.00961.14390.0086-0.06690.00690.11510.0433-0.3348-0.03650.3008-0.05190.08870.0071-0.01080.2369-0.0290.132326.08858.09842.554
742.30323.085310.046210.35732.238611.875-0.12861.43780.5225-0.65310.4294-0.68530.06931.0234-0.30080.2258-0.0080.17270.29230.00070.178827.47960.41616.701
81.4125-0.2721-0.51821.85140.74712.6248-0.055-0.04730.07480.1275-0.0276-0.10110.04940.08390.08260.1365-0.00780.00640.1134-0.00340.08769.0564.22440.069
91.1829-0.0636-0.48161.2143-0.27930.84490.00540.01030.29730.00690.037-0.237-0.20220.2149-0.04240.1835-0.04120.00610.1342-0.0060.125913.88176.30239.761
101.5285-0.32450.52051.6440.13972.9064-0.00740.06570.2313-0.08560.0221-0.412-0.40590.2171-0.01470.1207-0.06460.01130.1791-0.02480.172725.01671.10839.314
1110.3492-9.9689-3.567337.04721.85587.73070.2309-2.18990.240.96280.59-0.8899-0.21720.8298-0.8211.0324-0.2821-0.30350.8378-0.12290.312229.8678.39666.405
124.8327-5.0563-4.01026.69935.617111.6024-0.1407-0.43810.48530.11210.4057-0.8935-0.75380.7989-0.26490.2172-0.0947-0.14030.3569-0.03640.338332.54470.50454.379
132.1066-0.7966-0.811413.228211.283412.2668-0.1465-0.0501-0.0199-0.19230.259-0.3147-0.19250.7304-0.11240.08080.03220.03970.3337-0.02690.249735.32555.47536.214
140.3126-0.9340.21893.28760.05841.9090.09510.12390.0345-0.3102-0.0183-0.28860.05380.4576-0.07680.17050.03230.10530.3522-0.08480.20424.46249.88523.032
1525.986-6.705510.43392.2712-1.839111.44090.51531.6243-0.431-0.4863-0.52920.34950.3281-0.06610.01390.41580.0118-0.06560.3076-0.0770.26617.3345.13220.218
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A0 - 33
2X-RAY DIFFRACTION2A34 - 59
3X-RAY DIFFRACTION3A60 - 107
4X-RAY DIFFRACTION4A108 - 114
5X-RAY DIFFRACTION5A115 - 128
6X-RAY DIFFRACTION6A129 - 201
7X-RAY DIFFRACTION7A202 - 207
8X-RAY DIFFRACTION8A208 - 247
9X-RAY DIFFRACTION9A248 - 329
10X-RAY DIFFRACTION10A330 - 360
11X-RAY DIFFRACTION11A361 - 387
12X-RAY DIFFRACTION12A388 - 404
13X-RAY DIFFRACTION13A405 - 417
14X-RAY DIFFRACTION14A418 - 435
15X-RAY DIFFRACTION15A436 - 443

+
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