[English] 日本語
Yorodumi
- PDB-4a7q: Structure of human I113T SOD1 mutant complexed with 4-(4-methyl-1... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4a7q
TitleStructure of human I113T SOD1 mutant complexed with 4-(4-methyl-1,4- diazepan-1-yl)quinazoline in the p21 space group.
ComponentsSUPEROXIDE DISMUTASE [CU-ZN]
KeywordsOXIDOREDUCTASE / AMYOTROPHIC LATERAL SCLEROSIS / ANTIOXIDANT / DISEASE MUTATION / METAL-BINDING / ZN SUPEROXIDE DISMUTASE
Function / homology
Function and homology information


positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / action potential initiation / regulation of T cell differentiation in thymus / response to antipsychotic drug / neurofilament cytoskeleton organization / response to carbon monoxide / regulation of organ growth / relaxation of vascular associated smooth muscle / peripheral nervous system myelin maintenance / response to superoxide ...positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / action potential initiation / regulation of T cell differentiation in thymus / response to antipsychotic drug / neurofilament cytoskeleton organization / response to carbon monoxide / regulation of organ growth / relaxation of vascular associated smooth muscle / peripheral nervous system myelin maintenance / response to superoxide / anterograde axonal transport / protein phosphatase 2B binding / dense core granule / Oxidoreductases; Acting on a sulfur group of donors / regulation of GTPase activity / auditory receptor cell stereocilium organization / retina homeostasis / hydrogen peroxide biosynthetic process / cellular response to potassium ion / retrograde axonal transport / myeloid cell homeostasis / superoxide anion generation / muscle cell cellular homeostasis / superoxide metabolic process / response to copper ion / superoxide dismutase / Detoxification of Reactive Oxygen Species / heart contraction / superoxide dismutase activity / cellular response to cadmium ion / regulation of multicellular organism growth / cellular response to ATP / negative regulation of reproductive process / negative regulation of developmental process / transmission of nerve impulse / response to axon injury / ectopic germ cell programmed cell death / ovarian follicle development / neuronal action potential / embryo implantation / positive regulation of superoxide anion generation / axon cytoplasm / removal of superoxide radicals / reactive oxygen species metabolic process / thymus development / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / placenta development / positive regulation of phagocytosis / dendrite cytoplasm / response to amphetamine / determination of adult lifespan / positive regulation of cytokine production / regulation of mitochondrial membrane potential / glutathione metabolic process / response to hydrogen peroxide / sensory perception of sound / locomotory behavior / response to nutrient levels / negative regulation of inflammatory response / mitochondrial intermembrane space / regulation of blood pressure / small GTPase binding / Platelet degranulation / peroxisome / response to heat / protein-folding chaperone binding / gene expression / cytoplasmic vesicle / spermatogenesis / negative regulation of neuron apoptotic process / intracellular iron ion homeostasis / response to ethanol / positive regulation of MAPK cascade / lysosome / response to xenobiotic stimulus / positive regulation of apoptotic process / mitochondrial matrix / copper ion binding / neuronal cell body / apoptotic process / protein homodimerization activity / protein-containing complex / mitochondrion / : / extracellular exosome / extracellular region / zinc ion binding / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Superoxide dismutase, copper/zinc binding domain / Copper/Zinc superoxide dismutase signature 1. / Superoxide dismutase (Cu/Zn) / superoxide dismutase copper chaperone / Superoxide dismutase, copper/zinc, binding site / Copper/Zinc superoxide dismutase signature 2. / Superoxide dismutase, copper/zinc binding domain / Copper/zinc superoxide dismutase (SODC) / Superoxide dismutase-like, copper/zinc binding domain superfamily / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
4-(4-METHYL-1,4-DIAZEPAN-1-YL)QUINAZOLINE / COPPER (II) ION / Superoxide dismutase [Cu-Zn]
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / OTHER / Resolution: 1.22 Å
AuthorsWright, G.S.A. / Kershaw, N.M. / Antonyuk, S.V. / Strange, R.W. / ONeil, P.M. / Hasnain, S.S.
CitationJournal: Curr.Med.Chem. / Year: 2013
Title: X-Ray Crystallography and Computational Docking for the Detection and Development of Protein-Ligand Interactions.
Authors: Kershaw, N.M. / Wright, G.S. / Sharma, R. / Antonyuk, S.V. / Strange, R.W. / Berry, N.G. / O'Neill, P.M. / Hasnain, S.S.
History
DepositionNov 14, 2011Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 24, 2012Provider: repository / Type: Initial release
Revision 1.1Mar 13, 2013Group: Database references
Revision 1.2Aug 28, 2013Group: Database references
Revision 1.3Nov 13, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_entry_details / pdbx_modification_feature / pdbx_struct_conn_angle / struct_conn / 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_entry_details.has_protein_modification / _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.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.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_ptnr1_label_alt_id / _struct_conn.pdbx_ptnr2_label_alt_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_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_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: SUPEROXIDE DISMUTASE [CU-ZN]
F: SUPEROXIDE DISMUTASE [CU-ZN]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,95014
Polymers31,6312
Non-polymers1,31912
Water8,593477
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2480 Å2
ΔGint-96 kcal/mol
Surface area14220 Å2
MethodPISA
Unit cell
Length a, b, c (Å)38.010, 68.210, 49.010
Angle α, β, γ (deg.)90.00, 104.11, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

-
Protein , 1 types, 2 molecules AF

#1: Protein SUPEROXIDE DISMUTASE [CU-ZN] / SUPEROXIDE DISMUTASE-1 / SUPEROXIDE DISMUTASE 1 / HSOD1


Mass: 15815.508 Da / Num. of mol.: 2 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P00441, superoxide dismutase

-
Non-polymers , 5 types, 489 molecules

#2: Chemical ChemComp-4MQ / 4-(4-METHYL-1,4-DIAZEPAN-1-YL)QUINAZOLINE


Mass: 242.320 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C14H18N4
#3: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: SO4
#4: Chemical ChemComp-CU / COPPER (II) ION


Mass: 63.546 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cu
#5: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 477 / Source method: isolated from a natural source / Formula: H2O

-
Details

Compound detailsENGINEERED RESIDUE IN CHAIN A, ILE 114 TO THR ENGINEERED RESIDUE IN CHAIN F, ILE 114 TO THR
Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 1.79 Å3/Da / Density % sol: 31.32 % / Description: NONE
Crystal growpH: 5
Details: 100 MM SODIUM ACETATE PH 5, 150 MM SODIUM CHLORIDE, 2.5 AMMONIUM SULPHATE

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 1 / Wavelength: 0.787
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Jun 2, 2010 / Details: MIRRORS
RadiationMonochromator: SI111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.787 Å / Relative weight: 1
ReflectionResolution: 1.22→39 Å / Num. obs: 70164 / % possible obs: 97.3 % / Observed criterion σ(I): 0 / Redundancy: 3.5 % / Biso Wilson estimate: 14.3 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 9.7
Reflection shellResolution: 1.22→1.29 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.52 / Mean I/σ(I) obs: 1.9 / % possible all: 87.2

-
Processing

Software
NameVersionClassification
REFMAC5.5.0102refinement
XDSdata reduction
XDSdata scaling
REFMACphasing
RefinementMethod to determine structure: OTHER
Starting model: NONE

Resolution: 1.22→39 Å / Cor.coef. Fo:Fc: 0.98 / Cor.coef. Fo:Fc free: 0.97 / SU B: 1.394 / SU ML: 0.028 / Cross valid method: THROUGHOUT / ESU R: 0.042 / ESU R Free: 0.042 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY.
RfactorNum. reflection% reflectionSelection details
Rfree0.15925 3519 5 %RANDOM
Rwork0.12488 ---
obs0.12664 66844 100 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 10.156 Å2
Baniso -1Baniso -2Baniso -3
1-0.45 Å20 Å20 Å2
2---0.23 Å20 Å2
3----0.22 Å2
Refinement stepCycle: LAST / Resolution: 1.22→39 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2218 0 70 477 2765
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0140.0212570
X-RAY DIFFRACTIONr_bond_other_d0.0010.021672
X-RAY DIFFRACTIONr_angle_refined_deg1.6381.973517
X-RAY DIFFRACTIONr_angle_other_deg0.95334140
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.6755359
X-RAY DIFFRACTIONr_dihedral_angle_2_deg38.70125.78109
X-RAY DIFFRACTIONr_dihedral_angle_3_deg11.05315415
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.5671510
X-RAY DIFFRACTIONr_chiral_restr0.1050.2372
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.023083
X-RAY DIFFRACTIONr_gen_planes_other0.0020.02481
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_it1.6711.51657
X-RAY DIFFRACTIONr_mcbond_other0.5491.5706
X-RAY DIFFRACTIONr_mcangle_it2.49222679
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it3.4443913
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it4.9114.5838
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr1.39834242
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.218→1.25 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.234 211 -
Rwork0.207 4006 -
obs--100 %

+
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