[English] 日本語
Yorodumi
- PDB-7v0i: Crystal structure of a CelR catalytic domain active site mutant w... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7v0i
TitleCrystal structure of a CelR catalytic domain active site mutant with bound cellohexaose substrate
ComponentsGlucanase
KeywordsHYDROLASE/SUBSTRATE / biomass deconstruction / glycoside hydrolase family 9 / GH9 / cellulose binding domain 3c / CBM3c / HYDROLASE / HYDROLASE-SUBSTRATE complex
Function / homology
Function and homology information


Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds / cellulose binding / cellulose catabolic process / hydrolase activity, hydrolyzing O-glycosyl compounds / metal ion binding
Similarity search - Function
Glycoside hydrolase family 9, His active site / Glycosyl hydrolases family 9 (GH9) active site signature 2. / Glycosyl hydrolases family 9, Asp/Glu active sites / Glycosyl hydrolases family 9 (GH9) active site signature 3. / Cellulose binding domain / Carbohydrate-binding module 3 / Cellulose binding domain / CBM3 (carbohydrate binding type-3) domain profile. / Carbohydrate-binding module 3 superfamily / Glycoside hydrolase family 9 ...Glycoside hydrolase family 9, His active site / Glycosyl hydrolases family 9 (GH9) active site signature 2. / Glycosyl hydrolases family 9, Asp/Glu active sites / Glycosyl hydrolases family 9 (GH9) active site signature 3. / Cellulose binding domain / Carbohydrate-binding module 3 / Cellulose binding domain / CBM3 (carbohydrate binding type-3) domain profile. / Carbohydrate-binding module 3 superfamily / Glycoside hydrolase family 9 / Glycosyl hydrolase family 9 / Clostridium cellulosome enzymes repeated domain signature. / Dockerin domain / Dockerin domain profile. / Dockerin type I domain / Dockerin type I repeat / Dockerin domain superfamily / CBM2/CBM3, carbohydrate-binding domain superfamily / Six-hairpin glycosidase-like superfamily / Six-hairpin glycosidase superfamily / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain.
Similarity search - Domain/homology
Biological speciesAcetivibrio thermocellus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.9 Å
AuthorsBingman, C.A. / Kuch, N. / Kutsche, M.E. / Parker, A. / Smith, R.W. / Fox, B.G.
Funding support United States, 2items
OrganizationGrant numberCountry
Department of Energy (DOE, United States)DE-SC0018409 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)T32GM008349 United States
CitationJournal: J.Biol.Chem. / Year: 2023
Title: Contribution of calcium ligands in substrate binding and product release in the Acetovibrio thermocellus glycoside hydrolase family 9 cellulase CelR.
Authors: Kuch, N.J. / Kutschke, M.E. / Parker, A. / Bingman, C.A. / Fox, B.G.
History
DepositionMay 10, 2022Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 5, 2023Provider: repository / Type: Initial release
Revision 1.1May 3, 2023Group: Database references / Category: citation / Item: _citation.journal_volume
Revision 1.2Oct 25, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Glucanase
B: Glucanase
C: Glucanase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)163,2289
Polymers160,1353
Non-polymers3,0936
Water11,854658
1
A: Glucanase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)54,4093
Polymers53,3781
Non-polymers1,0312
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Glucanase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)54,4093
Polymers53,3781
Non-polymers1,0312
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Glucanase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)54,4093
Polymers53,3781
Non-polymers1,0312
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)93.302, 162.419, 210.522
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number20
Space group name H-MC2221
Components on special symmetry positions
IDModelComponents
11A-642-

HOH

-
Components

#1: Protein Glucanase


Mass: 53378.281 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Acetivibrio thermocellus (bacteria) / Gene: Cthe_0578 / Production host: Escherichia coli (E. coli)
References: UniProt: A3DCY5, Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
#2: Polysaccharide beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D- ...beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose


Type: oligosaccharide / Mass: 990.860 Da / Num. of mol.: 3 / Source method: obtained synthetically
DescriptorTypeProgram
DGlcpb1-4DGlcpb1-4DGlcpb1-4DGlcpb1-4DGlcpb1-4DGlcpb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,6,5/[a2122h-1b_1-5]/1-1-1-1-1-1/a4-b1_b4-c1_c4-d1_d4-e1_e4-f1WURCSPDB2Glycan 1.1.0
[][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{}}}}}}LINUCSPDB-CARE
#3: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Ca / Feature type: SUBJECT OF INVESTIGATION
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 658 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.49 Å3/Da / Density % sol: 50.61 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop
Details: JCSGD2B, 0.2M magnesium chloride, 0.1M HEPES buffer, pH 7.5, 30% PEG 400

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-G / Wavelength: 0.97856 Å
DetectorType: RAYONIX MX-300 / Detector: CCD / Date: Sep 19, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97856 Å / Relative weight: 1
ReflectionResolution: 1.9→39.87 Å / Num. obs: 125496 / % possible obs: 100 % / Redundancy: 7.471 % / Biso Wilson estimate: 34.16 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.077 / Rrim(I) all: 0.082 / Χ2: 0.889 / Net I/σ(I): 16.86 / Num. measured all: 937581 / Scaling rejects: 40
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsCC1/2Rrim(I) all% possible all
1.9-1.957.5071.3481.469143921692110.5951.44699.9
1.95-27.5311.0371.8767384894889470.7241.113100
2-2.067.5450.7762.5765772871887170.8210.833100
2.06-2.127.5390.613.3564096850385020.8760.654100
2.12-2.197.5630.484.3562194822382230.9150.515100
2.19-2.277.5490.3935.4560187797379730.940.421100
2.27-2.367.5310.3126.8957761767076700.9630.335100
2.36-2.457.5640.2428.8456243743674360.9750.26100
2.45-2.567.5290.19311.2553253707370730.9830.207100
2.56-2.697.5410.15214.4251465682568250.9890.163100
2.69-2.837.5140.12417.548676647964780.9920.133100
2.83-37.4810.09322.6845981614661460.9950.1100
3-3.217.4370.07228.243022578557850.9970.077100
3.21-3.477.3470.05435.7239658539853980.9980.058100
3.47-3.87.330.04243.1836347496049590.9990.045100
3.8-4.257.3070.03549.533152453745370.9990.037100
4.25-4.917.3130.0352.4429338401240120.9990.032100
4.91-6.017.3010.02851.7824822340034000.9990.03100
6.01-8.57.1880.02353.9119337269126900.9990.025100
8.5-39.876.440.02252.989750155015140.9990.02497.7

-
Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation1.9 Å39.87 Å
Translation1.9 Å39.87 Å

-
Processing

Software
NameVersionClassification
PHENIX1.20.1-4487refinement
XDSFeb 5, 2021 BUILT=20210322data reduction
XSCALEFeb 5, 2021 BUILT=20210322data scaling
PHASER2.8.3phasing
PDB_EXTRACT3.27data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 7UNP
Resolution: 1.9→39.87 Å / SU ML: 0.26 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 24.64 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2324 3037 2.41 %
Rwork0.1854 122807 -
obs0.1865 125496 99.8 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 206.4 Å2 / Biso mean: 49.4363 Å2 / Biso min: 21.02 Å2
Refinement stepCycle: final / Resolution: 1.9→39.87 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10782 0 375 660 11817
Biso mean--65.18 43.89 -
Num. residues----1353
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 22

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.9-1.930.35161540.3235359551397
1.93-1.960.30511530.303155175670100
1.96-1.990.33161530.295155575710100
1.99-2.030.33321500.291155355685100
2.03-2.070.3116820.275355615643100
2.07-2.110.335790.265455965675100
2.11-2.160.30221520.254255395691100
2.16-2.210.31181550.246455085663100
2.21-2.260.30381500.239155825732100
2.26-2.320.28381540.225955285682100
2.32-2.390.27111520.21655625714100
2.39-2.470.27421500.2255685718100
2.47-2.560.25121530.211755285681100
2.56-2.660.28281400.200255985738100
2.66-2.780.3327140.201957025716100
2.78-2.920.26041500.201856095759100
2.93-3.110.23321480.197855715719100
3.11-3.350.22081510.186956165767100
3.35-3.680.22471510.163355955746100
3.68-4.220.17831490.141556535802100
4.22-5.310.17441510.127456845835100
5.31-39.870.19011460.15185839598599
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)
10.4148-0.15520.27120.3758-0.34021.0879-0.1921-0.4139-0.59910.1104-0.2291-0.55590.31660.27230.32040.46310.11570.13060.43860.26540.652310.791-64.502-20.287
22.3384-0.7106-0.17371.6113-0.44812.3105-0.1128-0.6603-0.35370.2657-0.0799-0.11930.28260.11640.15520.48670.02190.12520.49930.13990.3801-5.745-61.099-9.703
32.01940.20670.46092.43-0.88964.578-0.2274-0.2242-0.19760.06570.17240.32880.5656-0.998-0.02990.2951-0.03340.13050.3256-0.02870.3347-20.632-56.569-23.394
41.97571.2261-0.91173.0044-1.82482.4707-0.15320.1053-0.0986-0.28720.00420.1280.0707-0.24250.1620.32460.02120.04970.2902-0.02770.235-9.982-49.182-37.222
50.50650.0538-0.08230.8986-0.10231.1662-0.1131-0.0146-0.2475-0.0765-0.01640.13360.2563-0.29240.10880.3931-0.03480.09890.3162-0.01020.3768-11.358-61.79-28.041
65.20014.08834.16155.54995.58375.6016-0.4316-0.56210.85710.68860.1354-0.847-0.25940.40790.38260.86380.087-0.17670.3744-0.09320.801-5.829-25.678-25.264
75.3928-0.97695.45089.3498-0.02778.6399-0.7672-1.71980.2755-0.1182-0.2551-0.40760.7463-0.85220.90020.59760.1860.12020.72310.03360.43816.787-32.308-28.473
80.70911.4076-2.09632.763-4.11066.0974-0.6495-0.16830.08760.2182-0.9181-0.4010.185-0.0161.4140.4368-0.04430.05530.63890.02560.59040.022-48.334-25.883
91.4784-0.5892-0.41812.70690.45021.26240.08370.04840.0871-0.1324-0.19460.2819-0.1196-0.22790.10280.29860.0815-0.05250.3708-0.12380.3206-20.926-19.771-32.236
102.4559-1.34280.51833.745-1.19833.1148-0.0265-0.1515-0.08260.4058-0.14590.41510.0144-0.33980.16190.35540.0210.05850.4032-0.15830.3343-25.503-22.084-18.189
111.290.4926-0.51492.06510.18541.7278-0.0655-0.63110.26830.42640.01750.01290.08920.11910.01170.48760.0906-0.03120.5619-0.23680.3934-11.725-11.258-10.603
121.2952-0.3841-0.44853.13692.12643.2070.0844-0.08970.4313-0.25750.1374-0.2166-0.38950.2457-0.22320.30330.01440.00620.2261-0.0670.3224-2.764-11.401-34.511
132.5315-1.5193-0.73735.69280.63741.57970.1932-0.07180.5927-0.3671-0.07760.0927-0.4089-0.0981-0.11880.42870.0484-0.01360.2785-0.11910.4087-10.816-6.535-31.836
142.31550.137-0.0041.28150.11271.3229-0.14580.11570.149-0.1720.0037-0.1863-0.29980.43150.1410.3303-0.0942-0.00150.39090.05340.244128.832-22.8-38.04
154.7741-0.5662-0.20671.3961.65122.9213-0.1857-0.4390.7523-0.03010.06660.0784-0.37490.22910.10930.3457-0.0841-0.06140.363-0.01250.282726.741-15.228-24.657
161.6490.24480.26431.57430.53591.8209-0.0569-0.4222-0.14640.2223-0.0773-0.29-0.02230.49520.09840.24910.0185-0.02150.5680.1260.305634.346-35.036-19.932
174.0142-0.69581.39592.6598-1.36471.5433-0.11780.3158-0.3556-0.44480.0755-0.14930.34250.11480.06530.2878-0.00450.07230.254-0.03850.203518.581-40.84-43.721
182.9688-0.2260.44121.93530.22520.9381-0.09830.0907-0.3358-0.4567-0.0377-0.51380.09640.55530.07580.27490.03790.10140.48890.07780.36734.655-38.457-37.123
191.55281.0881-0.12921.7791-0.4281.0133-0.3514-0.0231-0.5859-0.38510.0352-0.35310.54870.01650.21590.50680.060.24390.22880.02920.45830.751-64.082-33.556
207.62787.65343.02618.60194.5284.45730.33620.0517-0.86380.617-0.324-1.13980.82190.1247-0.01510.58260.17830.20030.3610.18830.62692.763-73.638-22.392
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN C AND RESID 190:229 )C190 - 229
2X-RAY DIFFRACTION2( CHAIN C AND RESID 230:353 )C230 - 353
3X-RAY DIFFRACTION3( CHAIN C AND RESID 354:392 )C354 - 392
4X-RAY DIFFRACTION4( CHAIN C AND RESID 393:445 )C393 - 445
5X-RAY DIFFRACTION5( CHAIN C AND RESID 446:469 )C446 - 469
6X-RAY DIFFRACTION6( CHAIN D AND RESID 1:6 )D1 - 6
7X-RAY DIFFRACTION7( CHAIN E AND RESID 1:6 )E1 - 6
8X-RAY DIFFRACTION8( CHAIN F AND RESID 1:6 )F1 - 6
9X-RAY DIFFRACTION9( CHAIN A AND RESID 19:167 )A19 - 167
10X-RAY DIFFRACTION10( CHAIN A AND RESID 168:229 )A168 - 229
11X-RAY DIFFRACTION11( CHAIN A AND RESID 230:353 )A230 - 353
12X-RAY DIFFRACTION12( CHAIN A AND RESID 354:432 )A354 - 432
13X-RAY DIFFRACTION13( CHAIN A AND RESID 433:469 )A433 - 469
14X-RAY DIFFRACTION14( CHAIN B AND RESID 19:189 )B19 - 189
15X-RAY DIFFRACTION15( CHAIN B AND RESID 190:229 )B190 - 229
16X-RAY DIFFRACTION16( CHAIN B AND RESID 230:392 )B230 - 392
17X-RAY DIFFRACTION17( CHAIN B AND RESID 393:432 )B393 - 432
18X-RAY DIFFRACTION18( CHAIN B AND RESID 433:469 )B433 - 469
19X-RAY DIFFRACTION19( CHAIN C AND RESID 19:167 )C19 - 167
20X-RAY DIFFRACTION20( CHAIN C AND RESID 168:189 )C168 - 189

+
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