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Basic information

Entry
Database: PDB / ID: 4yyf
TitleThe crystal structure of a glycosyl hydrolase of GH3 family member from [Mycobacterium smegmatis str. MC2 155
ComponentsBeta-N-acetylhexosaminidase
KeywordsHYDROLASE / structural genomics / PSI-Biology / protein structure initiative / midwest center for structural genomics / MCSG
Function / homology
Function and homology information


beta-N-acetylhexosaminidase / hydrolase activity, hydrolyzing O-glycosyl compounds / carbohydrate metabolic process
Similarity search - Function
: / Glycoside hydrolase, family 3, N-terminal domain / Glycoside hydrolase, family 3, N-terminal / Glycoside hydrolase, family 3, N-terminal domain superfamily / Glycosyl hydrolase family 3 N terminal domain / Prokaryotic membrane lipoprotein lipid attachment site profile. / Glycoside hydrolase superfamily / TIM Barrel / Alpha-Beta Barrel / Alpha Beta
Similarity search - Domain/homology
ACETATE ION / FORMIC ACID / beta-N-acetylhexosaminidase
Similarity search - Component
Biological speciesMycobacterium smegmatis (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.92 Å
AuthorsTan, K. / Hatzos-Skintges, C. / Clancy, S. / Joachimiak, A. / Midwest Center for Structural Genomics (MCSG)
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM094585 United States
CitationJournal: To Be Published
Title: The crystal structure of a glycosyl hydrolase of GH3 family member from [Mycobacterium smegmatis str. MC2 155
Authors: Tan, K. / Hatzos-Skintges, C. / Clancy, S. / Joachimiak, A.
History
DepositionMar 23, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 8, 2015Provider: repository / Type: Initial release
Revision 1.1Sep 20, 2017Group: Author supporting evidence / Derived calculations ...Author supporting evidence / Derived calculations / Refinement description / Source and taxonomy
Category: entity_src_gen / pdbx_audit_support ...entity_src_gen / pdbx_audit_support / pdbx_struct_assembly / pdbx_struct_oper_list / software
Item: _entity_src_gen.pdbx_alt_source_flag / _pdbx_audit_support.funding_organization ..._entity_src_gen.pdbx_alt_source_flag / _pdbx_audit_support.funding_organization / _pdbx_struct_assembly.oligomeric_details / _pdbx_struct_oper_list.symmetry_operation / _software.classification
Revision 1.2Dec 25, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.3Nov 13, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / pdbx_struct_conn_angle / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _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.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_symmetry / _pdbx_struct_conn_angle.ptnr3_auth_asym_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.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_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.ptnr1_symmetry / _struct_conn.ptnr2_auth_asym_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_conn.ptnr2_symmetry

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Beta-N-acetylhexosaminidase
B: Beta-N-acetylhexosaminidase
C: Beta-N-acetylhexosaminidase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)112,92814
Polymers112,3663
Non-polymers56111
Water9,962553
1
A: Beta-N-acetylhexosaminidase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)37,6435
Polymers37,4551
Non-polymers1874
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Beta-N-acetylhexosaminidase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)37,7717
Polymers37,4551
Non-polymers3156
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: Beta-N-acetylhexosaminidase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)37,5152
Polymers37,4551
Non-polymers591
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)103.067, 130.941, 85.986
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212

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Components

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Protein , 1 types, 3 molecules ABC

#1: Protein Beta-N-acetylhexosaminidase


Mass: 37455.484 Da / Num. of mol.: 3 / Mutation: A291V
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) (bacteria)
Strain: ATCC 700084 / mc(2)155 / Gene: MSMEG_0361, MSMEI_0354, LJ00_01805 / Plasmid: pMCSG68 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21-Gold(DE3) / References: UniProt: A0QPD6, beta-N-acetylhexosaminidase

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Non-polymers , 5 types, 564 molecules

#2: Chemical
ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C2H3O2
#3: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Na
#4: Chemical ChemComp-FMT / FORMIC ACID


Mass: 46.025 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: CH2O2
#5: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 553 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.61 Å3/Da / Density % sol: 52.9 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop / pH: 7 / Details: 2.8M Sodium Acetate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97918 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Mar 15, 2015
RadiationMonochromator: Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 1.92→36.5 Å / Num. obs: 89349 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 6.1 % / Rmerge(I) obs: 0.093 / Net I/σ(I): 23.3
Reflection shellResolution: 1.92→1.95 Å / Redundancy: 6.1 % / Rmerge(I) obs: 0.771 / Mean I/σ(I) obs: 2.6 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX1.8.2_1309refinement
SBC-Collectdata collection
HKL-3000data scaling
HKL-3000phasing
RefinementMethod to determine structure: SAD / Resolution: 1.92→36.41 Å / SU ML: 0.19 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 20.26 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2101 4376 4.94 %Random selection
Rwork0.179 ---
obs0.1805 88553 99.05 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.92→36.41 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7044 0 36 553 7633
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0077202
X-RAY DIFFRACTIONf_angle_d1.119816
X-RAY DIFFRACTIONf_dihedral_angle_d12.0922548
X-RAY DIFFRACTIONf_chiral_restr0.0751153
X-RAY DIFFRACTIONf_plane_restr0.0051314
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.9199-1.94170.30261440.25712352X-RAY DIFFRACTION85
1.9417-1.96460.27671580.25082571X-RAY DIFFRACTION93
1.9646-1.98850.26951530.23562747X-RAY DIFFRACTION98
1.9885-2.01370.24471460.22462758X-RAY DIFFRACTION99
2.0137-2.04020.25261660.22122771X-RAY DIFFRACTION100
2.0402-2.06810.26711290.22282804X-RAY DIFFRACTION100
2.0681-2.09770.24991250.21972834X-RAY DIFFRACTION100
2.0977-2.1290.21161370.21142785X-RAY DIFFRACTION100
2.129-2.16230.24841500.19582819X-RAY DIFFRACTION100
2.1623-2.19770.22041430.19212808X-RAY DIFFRACTION100
2.1977-2.23560.23631500.19742790X-RAY DIFFRACTION100
2.2356-2.27620.25091550.192803X-RAY DIFFRACTION100
2.2762-2.320.21831280.19122802X-RAY DIFFRACTION100
2.32-2.36740.23871310.18132803X-RAY DIFFRACTION100
2.3674-2.41880.21771630.18282812X-RAY DIFFRACTION100
2.4188-2.47510.21871560.17422803X-RAY DIFFRACTION100
2.4751-2.5370.19821360.18032834X-RAY DIFFRACTION100
2.537-2.60550.2521470.18782825X-RAY DIFFRACTION100
2.6055-2.68220.21771420.17912812X-RAY DIFFRACTION100
2.6822-2.76870.18921320.17922817X-RAY DIFFRACTION100
2.7687-2.86760.23161830.17672820X-RAY DIFFRACTION100
2.8676-2.98240.18721390.18192840X-RAY DIFFRACTION100
2.9824-3.11810.2231520.18182822X-RAY DIFFRACTION100
3.1181-3.28240.19611500.172851X-RAY DIFFRACTION100
3.2824-3.48790.19341340.15322850X-RAY DIFFRACTION100
3.4879-3.75690.15611410.1432872X-RAY DIFFRACTION100
3.7569-4.13450.15541400.14262891X-RAY DIFFRACTION100
4.1345-4.73170.1781290.142903X-RAY DIFFRACTION100
4.7317-5.95720.1611460.17182935X-RAY DIFFRACTION100
5.9572-36.4170.24061710.20533043X-RAY DIFFRACTION100
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)
13.34710.55730.84653.28491.05491.83710.0412-0.1471-0.08680.0992-0.060.23790.0501-0.17580.03890.09450.0002-0.00420.09950.00620.131688.696750.953878.4874
21.7443-0.5666-1.37841.34440.51513.1458-0.0619-0.01420.1283-0.06550.06120.0938-0.1372-0.0094-0.02290.1327-0.0134-0.01550.1287-0.00310.185101.246753.462478.8493
31.3275-0.79440.74371.61230.13270.72530.00040.14480.048-0.3890.1582-0.207-0.15950.4011-0.19370.1729-0.06010.05580.23940.01080.1982118.486447.48667.6976
41.08670.1760.33811.01920.33141.7745-0.08890.1606-0.0723-0.24230.0532-0.12390.05110.1180.0360.1437-0.0240.04340.12630.00140.1209107.909640.163564.719
50.4966-0.1669-0.41781.5950.13760.9725-0.04050.2097-0.054-0.3444-0.06020.2381-0.048-0.15240.09070.1746-0.0389-0.05080.1632-0.01610.14889.795442.757863.5545
63.47370.45272.1943.1116-0.24673.5795-0.0888-0.08670.0841-0.00190.00970.23890.0904-0.20250.09590.1275-0.02820.03510.1114-0.00230.184285.86438.141777.8177
74.2109-0.1145-1.54040.7352-0.87253.4002-0.08830.21980.4012-0.14750.19210.1287-0.2434-0.1151-0.12340.1849-0.0677-0.06480.17710.05720.164163.380524.269367.4266
81.6798-0.63030.23452.758-0.65971.9388-0.16510.30180.169-0.26410.16990.0207-0.0825-0.08850.00910.1947-0.1054-0.03050.23690.03970.190676.042924.74165.3088
91.10750.7218-0.53371.6539-0.55740.6892-0.0789-0.007-0.1251-0.11330.0295-0.22120.05160.09310.04980.112-0.01820.00340.1486-0.00470.145682.235310.68378.3451
101.13080.04740.08551.2181-0.35481.5317-0.11270.1422-0.0976-0.15920.10820.06080.0917-0.09090.00070.0992-0.04170.00690.12830.00910.10765.30279.262675.8182
112.5803-0.07310.35750.62110.42413.1137-0.11540.08820.1741-0.14330.07850.1927-0.195-0.16570.01490.131-0.0064-0.0270.11770.04220.148956.937220.282276.2263
123.4284-0.594-0.83154.12261.28261.59770.01660.70910.01990.2748-0.0844-0.4677-0.08340.52970.06580.507-0.0646-0.04980.8420.00140.487495.940614.192445.7269
131.47520.0899-0.07761.21620.01921.46410.21580.1032-0.2612-0.0229-0.0136-0.42060.30350.7003-0.19640.60080.0701-0.11210.7299-0.06520.516486.4134-3.542141.8856
142.62850.9229-1.67862.877-0.42591.26570.0139-0.5955-0.44180.2877-0.0943-0.60770.25620.42310.05610.67810.0707-0.20180.65080.01030.460783.9429-8.14549.0236
150.99830.0046-0.15060.83730.14310.87250.0455-0.0176-0.15470.0476-0.03210.01690.26070.0354-0.00210.5968-0.0486-0.05450.5328-0.0120.348569.7538-0.295543.5498
162.789-0.78051.18750.69740.47471.86480.2028-0.3122-0.1347-0.0337-0.0430.06280.09170.1337-0.19340.48160.0132-0.04880.57440.05810.338471.44910.065743.2055
171.05450.04720.50960.6484-0.18850.7664-0.03460.18290.1361-0.0996-0.0012-0.0573-0.11590.1740.0420.5565-0.0342-0.02580.6094-0.02120.34980.040316.405841.6049
180.8293-1.0335-0.65645.0471-0.99071.4974-0.0942-0.05750.29520.5848-0.023-0.6658-0.36410.70470.13650.6817-0.173-0.17240.728-0.02380.406587.481616.934554.2088
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 56 through 98 )
2X-RAY DIFFRACTION2chain 'A' and (resid 99 through 135 )
3X-RAY DIFFRACTION3chain 'A' and (resid 136 through 153 )
4X-RAY DIFFRACTION4chain 'A' and (resid 154 through 263 )
5X-RAY DIFFRACTION5chain 'A' and (resid 264 through 362 )
6X-RAY DIFFRACTION6chain 'A' and (resid 363 through 386 )
7X-RAY DIFFRACTION7chain 'B' and (resid 56 through 98 )
8X-RAY DIFFRACTION8chain 'B' and (resid 99 through 135 )
9X-RAY DIFFRACTION9chain 'B' and (resid 136 through 283 )
10X-RAY DIFFRACTION10chain 'B' and (resid 284 through 348 )
11X-RAY DIFFRACTION11chain 'B' and (resid 349 through 385 )
12X-RAY DIFFRACTION12chain 'C' and (resid 56 through 88 )
13X-RAY DIFFRACTION13chain 'C' and (resid 89 through 153 )
14X-RAY DIFFRACTION14chain 'C' and (resid 154 through 181 )
15X-RAY DIFFRACTION15chain 'C' and (resid 182 through 263 )
16X-RAY DIFFRACTION16chain 'C' and (resid 264 through 283 )
17X-RAY DIFFRACTION17chain 'C' and (resid 284 through 362 )
18X-RAY DIFFRACTION18chain 'C' and (resid 363 through 386 )

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