[English] 日本語
Yorodumi
- PDB-1xhu: HincII bound to cleaved, cognate DNA containing GTCGAC -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 1xhu
TitleHincII bound to cleaved, cognate DNA containing GTCGAC
Components
  • 5'-D(*GP*CP*CP*GP*GP*TP*C)-3'
  • 5'-D(P*GP*AP*CP*CP*GP*G)-3'
  • Type II restriction enzyme HincII
Keywordshydrolase/DNA / restriction endonuclease / phosphoryl transfer / hydrolase-DNA COMPLEX
Function / homology
Function and homology information


type II site-specific deoxyribonuclease / type II site-specific deoxyribonuclease activity / DNA restriction-modification system / DNA binding
Similarity search - Function
Restriction endonuclease, type II, HincII / Restriction endonuclease HincII / DNA mismatch repair MutH/Restriction endonuclease, type II / DNA mismatch repair MutH/Type II restriction endonuclease superfamily / ECO RV Endonuclease; Chain A / Restriction endonuclease type II-like / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
DNA / Type II restriction enzyme HincII
Similarity search - Component
Biological speciesHaemophilus influenzae (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.95 Å
AuthorsEtzkorn, C. / Horton, N.C.
CitationJournal: J.Mol.Biol. / Year: 2004
Title: Mechanistic Insights from the Structures of HincII Bound to Cognate DNA Cleaved from Addition of Mg(2+) and Mn(2+)
Authors: Etzkorn, C. / Horton, N.C.
History
DepositionSep 20, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 28, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 11, 2017Group: Refinement description / Category: software / Item: _software.classification / _software.name
Revision 1.4Aug 23, 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 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
E: 5'-D(*GP*CP*CP*GP*GP*TP*C)-3'
F: 5'-D(P*GP*AP*CP*CP*GP*G)-3'
G: 5'-D(*GP*CP*CP*GP*GP*TP*C)-3'
H: 5'-D(P*GP*AP*CP*CP*GP*G)-3'
I: 5'-D(*GP*CP*CP*GP*GP*TP*C)-3'
J: 5'-D(P*GP*AP*CP*CP*GP*G)-3'
K: 5'-D(*GP*CP*CP*GP*GP*TP*C)-3'
L: 5'-D(P*GP*AP*CP*CP*GP*G)-3'
A: Type II restriction enzyme HincII
B: Type II restriction enzyme HincII
C: Type II restriction enzyme HincII
D: Type II restriction enzyme HincII


Theoretical massNumber of molelcules
Total (without water)135,07512
Polymers135,07512
Non-polymers00
Water10,070559
1
E: 5'-D(*GP*CP*CP*GP*GP*TP*C)-3'
F: 5'-D(P*GP*AP*CP*CP*GP*G)-3'
G: 5'-D(*GP*CP*CP*GP*GP*TP*C)-3'
H: 5'-D(P*GP*AP*CP*CP*GP*G)-3'
A: Type II restriction enzyme HincII
B: Type II restriction enzyme HincII


Theoretical massNumber of molelcules
Total (without water)67,5376
Polymers67,5376
Non-polymers00
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
I: 5'-D(*GP*CP*CP*GP*GP*TP*C)-3'
J: 5'-D(P*GP*AP*CP*CP*GP*G)-3'
K: 5'-D(*GP*CP*CP*GP*GP*TP*C)-3'
L: 5'-D(P*GP*AP*CP*CP*GP*G)-3'
C: Type II restriction enzyme HincII
D: Type II restriction enzyme HincII


Theoretical massNumber of molelcules
Total (without water)67,5376
Polymers67,5376
Non-polymers00
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)67.20, 177.2, 256.0
Angle α, β, γ (deg.)90.0, 90.0, 90.0
Int Tables number24
Space group name H-MI212121

-
Components

#1: DNA chain
5'-D(*GP*CP*CP*GP*GP*TP*C)-3'


Mass: 2114.398 Da / Num. of mol.: 4 / Source method: obtained synthetically / Details: phosphoramidite synthetic chemistry
#2: DNA chain
5'-D(P*GP*AP*CP*CP*GP*G)-3'


Mass: 1834.230 Da / Num. of mol.: 4 / Source method: obtained synthetically / Details: phosphoramidite synthetic chemistry
#3: Protein
Type II restriction enzyme HincII / Endonuclease HincII / R.HincII


Mass: 29820.066 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Haemophilus influenzae (bacteria) / Gene: hincIIR / Production host: Escherichia coli (E. coli)
References: UniProt: P17743, type II site-specific deoxyribonuclease
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 559 / 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: 2.82 Å3/Da / Density % sol: 56.4 %
Crystal growTemperature: 290 K / Method: vapor diffusion, hanging drop / pH: 5.5
Details: PEG 4000, NaCl, citrate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K
Components of the solutions
IDNameCrystal-IDSol-ID
1PEG 400011
2NaCl11
3citrate11

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL9-1 / Wavelength: 0.9 Å
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9 Å / Relative weight: 1
ReflectionResolution: 2.95→50 Å / Num. obs: 27364 / % possible obs: 85.4 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 2.3 % / Biso Wilson estimate: 46.2 Å2 / Rmerge(I) obs: 0.078 / Rsym value: 0.078 / Net I/σ(I): 6.1

-
Processing

Software
NameVersionClassification
XDSdata scaling
SCALAdata scaling
CNSrefinement
XDSdata reduction
CCP4(SCALA)data scaling
CNSphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1KC6 with water removed

1kc6


Resolution: 2.95→50 Å / Cross valid method: R free / σ(F): 3 / Stereochemistry target values: as in CNS
RfactorNum. reflection% reflectionSelection details
Rfree0.277 1368 -5% random
Rwork0.187 ---
all-27364 --
obs-23369 85.4 %-
Refinement stepCycle: LAST / Resolution: 2.95→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8135 1064 0 559 9758
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.009
X-RAY DIFFRACTIONc_angle_deg1.38

+
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