[English] 日本語
Yorodumi
- PDB-10ei: GH33 sialidase from Alistipes dispar in complex with free sialic acid -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 10ei
TitleGH33 sialidase from Alistipes dispar in complex with free sialic acid
Componentsexo-alpha-sialidase
KeywordsHYDROLASE / Glycoside hydrolase
Function / homology
Function and homology information


ganglioside catabolic process / oligosaccharide catabolic process / exo-alpha-sialidase / exo-alpha-sialidase activity / membrane / cytoplasm
Similarity search - Function
BNR repeat-like domain / Sialidase family / Sialidase / Sialidase superfamily / Prokaryotic membrane lipoprotein lipid attachment site profile.
Similarity search - Domain/homology
N-acetyl-alpha-neuraminic acid / exo-alpha-sialidase
Similarity search - Component
Biological speciesAlistipes dispar (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.49 Å
AuthorsPlisko, O.L. / Redinbo, M.R.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35 GM152079 United States
CitationJournal: To Be Published
Title: Distinct Processing of Human Milk Oligosaccharides by Early Life Human Gut Microbial Sialidases
Authors: Maurer, O.L. / Chapel, V.C. / Sekela, J.J. / Talbert, J. / Townsend, S. / Zemel, B.S. / Wu, G.D. / Redinbo, M.R.
History
DepositionJan 15, 2026Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 21, 2026Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: exo-alpha-sialidase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,4824
Polymers41,9881
Non-polymers4933
Water5,296294
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)90.480, 90.480, 82.941
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number154
Space group name H-MP3221
Space group name HallP322"
Symmetry operation#1: x,y,z
#2: -y,x-y,z+2/3
#3: -x+y,-x,z+1/3
#4: x-y,-y,-z+1/3
#5: -x,-x+y,-z+2/3
#6: y,x,-z
Components on special symmetry positions
IDModelComponents
11A-756-

HOH

21A-778-

HOH

31A-793-

HOH

-
Components

#1: Protein exo-alpha-sialidase


Mass: 41988.219 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Alistipes dispar (bacteria) / Gene: nanH, A5CPEGH6_05410 / Plasmid: pLIC-His / Production host: Escherichia coli (E. coli) / References: UniProt: A0A4Y1WXT9, exo-alpha-sialidase
#2: Sugar ChemComp-SIA / N-acetyl-alpha-neuraminic acid / N-acetylneuraminic acid / sialic acid / alpha-sialic acid / O-SIALIC ACID


Type: D-saccharide, alpha linking / Mass: 309.270 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C11H19NO9 / Feature type: SUBJECT OF INVESTIGATION
IdentifierTypeProgram
DNeup5AcaCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-a-D-neuraminic acidCOMMON NAMEGMML 1.0
a-D-Neup5AcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
Neu5AcSNFG CARBOHYDRATE SYMBOLGMML 1.0
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 294 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationN

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.25 Å3/Da / Density % sol: 45.3 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 4
Details: 0.1 M Sodium Citrate:HCl pH 4, 0.8 M Ammonium sulfate

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: NSLS-II / Beamline: 17-ID-1 / Wavelength: 1 Å
DetectorType: DECTRIS EIGER X 9M / Detector: PIXEL / Date: Nov 27, 2023
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.49→29.62 Å / Num. obs: 64525 / % possible obs: 100 % / Redundancy: 10.3 % / Biso Wilson estimate: 21.41 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.086 / Rpim(I) all: 0.028 / Rrim(I) all: 0.0909 / Net I/σ(I): 13
Reflection shellResolution: 1.49→1.54 Å / Redundancy: 10.4 % / Rmerge(I) obs: 2.104 / Mean I/σ(I) obs: 0.91 / Num. unique obs: 6381 / CC1/2: 0.38 / Rpim(I) all: 0.686 / Rrim(I) all: 2.215 / % possible all: 100

-
Processing

Software
NameVersionClassification
autoPROCdata reduction
Aimlessdata scaling
PHASERphasing
PHENIX1.21_5207refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.49→29.62 Å / SU ML: 0.2191 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 24.8256
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2069 1992 3.09 %
Rwork0.1908 62531 -
obs0.1913 64523 99.99 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 26.84 Å2
Refinement stepCycle: LAST / Resolution: 1.49→29.62 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2729 0 33 294 3056
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00532849
X-RAY DIFFRACTIONf_angle_d0.93133892
X-RAY DIFFRACTIONf_chiral_restr0.0826424
X-RAY DIFFRACTIONf_plane_restr0.0074515
X-RAY DIFFRACTIONf_dihedral_angle_d15.61431040
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.49-1.530.34061390.33074403X-RAY DIFFRACTION100
1.53-1.570.37991460.30994446X-RAY DIFFRACTION100
1.57-1.610.31661420.28314415X-RAY DIFFRACTION99.98
1.61-1.670.28791380.26364415X-RAY DIFFRACTION99.98
1.67-1.720.29341390.25234431X-RAY DIFFRACTION100
1.72-1.790.21791420.22514435X-RAY DIFFRACTION100
1.79-1.880.24021360.22824426X-RAY DIFFRACTION100
1.88-1.970.241440.20134463X-RAY DIFFRACTION100
1.97-2.10.2041440.20434434X-RAY DIFFRACTION100
2.1-2.260.23321410.18944478X-RAY DIFFRACTION100
2.26-2.490.19721430.20884471X-RAY DIFFRACTION100
2.49-2.850.21081440.19424501X-RAY DIFFRACTION99.98
2.85-3.590.19461400.1724528X-RAY DIFFRACTION99.94
3.59-29.620.16251540.15044685X-RAY DIFFRACTION99.98

+
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