[English] 日本語
Yorodumi
- PDB-4ysh: Crystal structure of glycine oxidase from Geobacillus kaustophilus -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4ysh
TitleCrystal structure of glycine oxidase from Geobacillus kaustophilus
ComponentsGlycine oxidase
KeywordsOXIDOREDUCTASE / flavoprotein / glycine oxidase / substrate inhibition
Function / homology
Function and homology information


glycine oxidase / glycine oxidase activity / thiamine diphosphate biosynthetic process / thiamine biosynthetic process / amino acid metabolic process / FAD binding / protein homotetramerization
Similarity search - Function
Glycine oxidase ThiO / FAD dependent oxidoreductase / FAD dependent oxidoreductase / D-Amino Acid Oxidase, subunit A, domain 2 / D-Amino Acid Oxidase; Chain A, domain 2 / FAD/NAD(P)-binding domain / FAD/NAD(P)-binding domain / 3-Layer(bba) Sandwich / FAD/NAD(P)-binding domain superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
FLAVIN-ADENINE DINUCLEOTIDE / GLYCINE / ISOPROPYL ALCOHOL / Glycine oxidase
Similarity search - Component
Biological speciesGeobacillus kaustophilus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.2 Å
AuthorsShiono, T. / Nomura, T. / Arai, R.
Funding support Japan, 1items
OrganizationGrant numberCountry
JSPSKAKENHI 24780097 Japan
CitationJournal: to be published
Title: Crystal structure of glycine oxidase from Geobacillus kaustophilus
Authors: Shiono, T. / Arai, R. / Nishiya, Y. / Nomura, T.
History
DepositionMar 17, 2015Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Mar 23, 2016Provider: repository / Type: Initial release
Revision 1.1Feb 5, 2020Group: Data collection / Derived calculations
Category: diffrn_source / pdbx_struct_oper_list / pdbx_struct_special_symmetry
Item: _diffrn_source.pdbx_synchrotron_site / _pdbx_struct_oper_list.symmetry_operation
Revision 1.2Nov 8, 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: Glycine oxidase
B: Glycine oxidase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)81,87411
Polymers79,7692
Non-polymers2,1059
Water3,315184
1
A: Glycine oxidase
B: Glycine oxidase
hetero molecules

A: Glycine oxidase
B: Glycine oxidase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)163,74822
Polymers159,5384
Non-polymers4,21018
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation8_555x-y,-y,-z1
Buried area14770 Å2
ΔGint-144 kcal/mol
Surface area53290 Å2
MethodPISA
Unit cell
Length a, b, c (Å)87.945, 87.945, 413.456
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number179
Space group name H-MP6522
SymmetryPoint symmetry: (Schoenflies symbol: C2 (2 fold cyclic))
Components on special symmetry positions
IDModelComponents
11B-406-

SO4

-
Components

-
Protein , 1 types, 2 molecules AB

#1: Protein Glycine oxidase


Mass: 39884.465 Da / Num. of mol.: 2 / Mutation: A139del
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Geobacillus kaustophilus (strain HTA426) (bacteria)
Strain: HTA426 / Gene: GK0623 / Plasmid: pET3a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: Q5L2C2, glycine oxidase

-
Non-polymers , 6 types, 193 molecules

#2: Chemical ChemComp-FAD / FLAVIN-ADENINE DINUCLEOTIDE


Mass: 785.550 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C27H33N9O15P2 / Comment: FAD*YM
#3: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: SO4
#4: Chemical ChemComp-GLY / GLYCINE


Type: peptide linking / Mass: 75.067 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H5NO2
#5: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#6: Chemical ChemComp-IPA / ISOPROPYL ALCOHOL / 2-PROPANOL


Mass: 60.095 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O / Comment: alkaloid*YM
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 184 / 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: 2.89 Å3/Da / Density % sol: 57.41 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4.7
Details: 0.1 M phosphate-citrate buffer, 7% 2-propanol, 0.4 M LiSO4

-
Data collection

DiffractionMean temperature: 95 K
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: AR-NE3A / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 270 / Detector: CCD / Date: Feb 1, 2014
RadiationMonochromator: Numerical link type Si(111) double crystal monochromator
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.2→50 Å / Num. obs: 48899 / % possible obs: 98.6 % / Redundancy: 20.6 % / Biso Wilson estimate: 34.4 Å2 / Rmerge(I) obs: 0.096 / Rpim(I) all: 0.022 / Rrim(I) all: 0.098 / Χ2: 1 / Net I/av σ(I): 32.785 / Net I/σ(I): 11.5 / Num. measured all: 1006443
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique allCC1/2Rpim(I) allRrim(I) allΧ2% possible all
2.2-2.2822.20.41710.547740.9720.0890.4260.95899.7
2.28-2.3722.10.35248320.9820.0750.361.00299.8
2.37-2.48220.26548140.9880.0570.2721.03299.8
2.48-2.6121.90.22948670.990.0490.2351.02699.8
2.61-2.7721.60.16948800.9940.0360.1731.03799.9
2.77-2.9921.40.12448940.9960.0270.1280.98399.9
2.99-3.2920.90.09749240.9970.0220.11.02999.9
3.29-3.7619.90.07549850.9980.0170.0770.965100
3.76-4.74180.06649970.9970.0160.0680.96798.3
4.74-5015.90.06449320.9970.0160.0660.99390.2

-
Phasing

PhasingMethod: molecular replacement

-
Processing

Software
NameVersionClassification
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
MOLREP10.2.35phasing
REFMAC5.5.0109refinement
PDB_EXTRACT3.15data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB 1RYI
Resolution: 2.2→50 Å / Cor.coef. Fo:Fc: 0.915 / Cor.coef. Fo:Fc free: 0.897 / WRfactor Rfree: 0.2682 / WRfactor Rwork: 0.2314 / FOM work R set: 0.8341 / SU B: 13.612 / SU ML: 0.163 / SU R Cruickshank DPI: 0.2666 / SU Rfree: 0.2137 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.267 / ESU R Free: 0.214 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.2661 2463 5.1 %RANDOM
Rwork0.2328 ---
obs0.2345 46153 98.34 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso max: 139.76 Å2 / Biso mean: 44.542 Å2 / Biso min: 24.03 Å2
Baniso -1Baniso -2Baniso -3
1-0.66 Å20.33 Å20 Å2
2--0.66 Å20 Å2
3----0.99 Å2
Refinement stepCycle: final / Resolution: 2.2→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5510 0 136 184 5830
Biso mean--42.88 45.06 -
Num. residues----738
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0090.0225807
X-RAY DIFFRACTIONr_angle_refined_deg1.3441.9957915
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.8045746
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.0522.356225
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.22715889
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.131549
X-RAY DIFFRACTIONr_chiral_restr0.1010.2891
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0214390
X-RAY DIFFRACTIONr_mcbond_it0.4291.53666
X-RAY DIFFRACTIONr_mcangle_it0.80425826
X-RAY DIFFRACTIONr_scbond_it1.09932141
X-RAY DIFFRACTIONr_scangle_it1.8854.52084
LS refinement shellResolution: 2.201→2.258 Å
RfactorNum. reflection% reflection
Rfree0.307 182 5.2 %
Rwork0.271 3321 -
obs--98.95 %
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)
14.72820.7273-0.29012.09130.57041.25810.0137-0.714-0.39640.266-0.12560.21420.1327-0.16440.11180.24530.05010.03490.47550.05850.2991-72.340612.722613.149
29.0896-1.88883.26124.0098-2.35822.8663-0.1152-0.29221.6267-0.1189-0.18260.0152-0.1092-0.15370.29770.15750.11030.0070.317-0.13590.4737-66.517428.31529.3723
30.966-0.72991.20474.4638-5.05267.950.0151-0.08050.1535-0.1771-0.02130.0718-0.341-0.3270.00620.36110.0976-0.02830.2795-0.00260.3346-57.875730.5968-2.6937
412.2496-6.6978-3.025610.29163.52895.7202-0.3403-0.28280.667-0.6217-0.0992-0.2187-0.8752-0.56360.43960.45910.1361-0.07780.1187-0.03570.2171-59.039241.5522-4.5562
51.7517-0.26180.09570.8367-0.27591.8846-0.04530.00670.1757-0.37250.1014-0.0854-0.1467-0.1688-0.05610.39830.05740.01730.3211-0.0240.3831-56.377625.90441.4097
67.78517.38070.15859.36250.77672.0647-0.3966-1.2481-2.59860.1128-0.09980.23710.0859-0.310.49630.01650.17130.33880.4050.61611.7255-80.41912.792212.0183
72.87160.504-0.73431.2234-0.22931.1209-0.11040.1626-0.0082-0.06520.03380.1764-0.0538-0.25360.07660.30050.07180.00560.3968-0.01930.2844-68.803116.4844-1.2493
82.17670.70260.13051.5441.05880.9870.05470.196-0.0845-0.1457-0.03620.0063-0.0984-0.2966-0.01860.32180.07060.02870.36740.02130.2986-56.969917.2739-9.8248
910.55372.2736-1.30411.7398-0.59712.01660.1755-0.0509-0.0839-0.1254-0.1735-0.095-0.1342-0.042-0.0020.3230.04870.01240.3244-0.0330.2824-52.460514.7361-7.7554
109.83672.1869-5.41674.1606-2.00417.1218-0.06570.50320.2844-0.06030.24970.37560.06-0.8297-0.1840.14650.09160.01610.50740.01160.3115-84.14619.06114.2397
116.54560.2819-0.99311.7706-1.12152.91690.0157-0.05380.76090.0159-0.11930.1734-0.314-0.49410.10360.17870.12580.00140.4042-0.11680.3981-78.998824.74258.1977
122.717-0.13760.49964.75841.24313.17430.06520.35230.1336-0.5140.0577-0.2923-0.33750.3569-0.12280.3562-0.04880.02310.3651-0.00510.2751-26.68918.55637.6845
130.80681.22741.32911.4534.04964.2458-0.31680.26540.3663-0.8912-0.09990.3029-0.83440.02920.41670.3634-0.06450.01270.41190.03870.3244-26.175623.90577.4493
140.9250.2345-0.28640.15390.13781.39660.06090.0187-0.1089-0.01410.0618-0.07830.0327-0.0145-0.12270.342-0.0331-0.00150.33-0.01290.334-33.50267.940521.9203
151.59910.0807-0.06921.1063-0.63782.06950.0257-0.0140.19180.0533-0.00620.0287-0.2657-0.1894-0.01950.3485-0.0042-0.00150.3391-0.01870.2926-43.613117.481821.2768
164.27761.22631.29571.16530.73032.2780.1101-0.2955-0.18950.1729-0.11090.0660.2135-0.39160.00080.3388-0.07440.0020.38940.01390.2432-44.30611.668240.6996
171.3058-0.1378-0.21580.80920.15842.0394-0.00390.1233-0.0454-0.11510.0101-0.07720.05270.0097-0.00630.3541-0.0204-0.02170.3439-0.02930.3433-34.454810.287513.6738
181.22760.22570.17430.8585-0.16324.1488-0.0060.2703-0.0743-0.33960.0477-0.2544-0.05620.3041-0.04170.3195-0.02670.07190.3968-0.07330.3197-20.83689.46043.971
192.44760.388-0.77590.62580.15781.3515-0.0311-0.101-0.13130.05590.0252-0.06980.1682-0.02380.00590.3098-0.022-0.03140.3425-0.00690.32-38.3077-0.318319.4434
203.17720.0681-0.54411.00220.25960.866-0.01960.0233-0.3026-0.04820.0078-0.10130.1464-0.07310.01180.3157-0.0453-0.01760.322-0.00980.3148-44.2686-5.264617.5239
213.54720.8899-0.27061.32750.62931.97270.0778-0.1231-0.12410.1212-0.06540.05730.0732-0.3662-0.01240.3048-0.05240.00230.3127-0.00650.2939-51.758-5.833419.726
223.56291.6133-0.78824.6029-1.11513.67760.0177-0.0081-0.24850.00270.0017-0.32270.0720.2568-0.01940.30390.0144-0.01630.3761-0.06440.3049-20.14656.837917.9403
232.49060.2514-0.38221.0099-0.27353.0657-0.0127-0.0137-0.1052-0.0040.0511-0.1748-0.07620.2181-0.03850.3308-0.0082-0.00110.3446-0.03880.3173-23.223913.580922.4263
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A2 - 53
2X-RAY DIFFRACTION2A54 - 83
3X-RAY DIFFRACTION3A84 - 107
4X-RAY DIFFRACTION4A108 - 134
5X-RAY DIFFRACTION5A135 - 166
6X-RAY DIFFRACTION6A167 - 197
7X-RAY DIFFRACTION7A198 - 251
8X-RAY DIFFRACTION8A252 - 293
9X-RAY DIFFRACTION9A294 - 308
10X-RAY DIFFRACTION10A309 - 332
11X-RAY DIFFRACTION11A333 - 371
12X-RAY DIFFRACTION12B2 - 25
13X-RAY DIFFRACTION13B26 - 32
14X-RAY DIFFRACTION14B33 - 69
15X-RAY DIFFRACTION15B70 - 97
16X-RAY DIFFRACTION16B98 - 136
17X-RAY DIFFRACTION17B137 - 189
18X-RAY DIFFRACTION18B190 - 213
19X-RAY DIFFRACTION19B214 - 249
20X-RAY DIFFRACTION20B250 - 286
21X-RAY DIFFRACTION21B287 - 307
22X-RAY DIFFRACTION22B308 - 334
23X-RAY DIFFRACTION23B335 - 369

+
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