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- PDB-2yjq: Structure of a Paenibacillus Polymyxa Xyloglucanase from Glycosid... -

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Basic information

Entry
Database: PDB / ID: 2yjq
TitleStructure of a Paenibacillus Polymyxa Xyloglucanase from Glycoside Hydrolase Family 44
ComponentsCEL44C
KeywordsHYDROLASE / GH44 / ENDO-GLUCANASE / CARBOHYDRATE-BINDING PROTEIN
Function / homology
Function and homology information


substituted mannan metabolic process / mannan endo-1,4-beta-mannosidase activity / cellulose binding / metal ion binding
Similarity search - Function
Glycoside hydrolase, family 44 / Glycoside hydrolase family 44 / Glycoside hydrolase family 26 / Carbohydrate binding module (family 35) / Glycosyl hydrolase family 26 / Glycosyl hydrolase family 26 domain / Glycosyl hydrolases family 26 (GH26) domain profile. / Cellulose binding domain / Cellulose binding domain / Carbohydrate-binding module 3 ...Glycoside hydrolase, family 44 / Glycoside hydrolase family 44 / Glycoside hydrolase family 26 / Carbohydrate binding module (family 35) / Glycosyl hydrolase family 26 / Glycosyl hydrolase family 26 domain / Glycosyl hydrolases family 26 (GH26) domain profile. / Cellulose binding domain / Cellulose binding domain / Carbohydrate-binding module 3 / Carbohydrate-binding module 3 superfamily / CBM3 (carbohydrate binding type-3) domain profile. / CBM6 (carbohydrate binding type-6) domain profile. / Carbohydrate binding module family 6 / CBM2/CBM3, carbohydrate-binding domain superfamily / Golgi alpha-mannosidase II / Glycosyl hydrolase, all-beta / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Galactose-binding-like domain superfamily / Fibronectin type III / Fibronectin type III superfamily / Glycosidases / Glycoside hydrolase superfamily / TIM Barrel / Alpha-Beta Barrel / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
beta-cellobiose / TETRAHYDROOXAZINE / TRIETHYLENE GLYCOL / Cel44C
Similarity search - Component
Biological speciesPAENIBACILLUS POLYMYXA (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.25 Å
AuthorsAriza, A. / Eklof, J.M. / Spadiut, O. / Offen, W.A. / Roberts, S.M. / Besenmatter, W. / Friis, E.P. / Skjot, M. / Wilson, K.S. / Brumer, H. / Davies, G.
CitationJournal: J.Biol.Chem. / Year: 2011
Title: Structure and Activity of Paenibacillus Polymyxa Xyloglucanase from Glycoside Hydrolase Family 44.
Authors: Ariza, A. / Eklof, J.M. / Spadiut, O. / Offen, W.A. / Roberts, S.M. / Besenmatter, W. / Friis, E.P. / Skjot, M. / Wilson, K.S. / Brumer, H. / Davies, G.
History
DepositionMay 23, 2011Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 15, 2011Provider: repository / Type: Initial release
Revision 1.1Apr 25, 2012Group: Database references / Other / Version format compliance
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Other / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / entity_name_com / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_database_status / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_molecule_features / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_alt_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.occupancy / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.src_method / _entity.type / _pdbx_database_status.status_code_sf / _pdbx_struct_assembly_gen.asym_id_list / _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.ptnr2_label_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.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.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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Remark 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AD" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AD" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BD" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: CEL44C
B: CEL44C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)117,92823
Polymers115,8312
Non-polymers2,09721
Water7,909439
1
A: CEL44C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)59,03912
Polymers57,9151
Non-polymers1,12411
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: CEL44C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)58,88911
Polymers57,9151
Non-polymers97310
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)84.200, 84.200, 320.050
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number154
Space group name H-MP3221

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Components

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Protein / Sugars , 2 types, 4 molecules AB

#1: Protein CEL44C / XYLOGLUCANASE


Mass: 57915.293 Da / Num. of mol.: 2 / Fragment: RESIDUES 36-559 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) PAENIBACILLUS POLYMYXA (bacteria) / Strain: GS01 / Production host: BACILLUS SUBTILIS (bacteria) / Strain (production host): SHA273
References: UniProt: Q1A2D0, cellulase, xyloglucan-specific endo-beta-1,4-glucanase
#2: Polysaccharide beta-D-glucopyranose-(1-4)-beta-D-glucopyranose / beta-cellobiose


Type: oligosaccharide, Oligosaccharide / Class: Metabolism / Mass: 342.297 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: oligosaccharide / References: beta-cellobiose
DescriptorTypeProgram
DGlcpb1-4DGlcpb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-Glcp]{[(4+1)][b-D-Glcp]{}}LINUCSPDB-CARE

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Non-polymers , 7 types, 458 molecules

#3: Chemical ChemComp-OXZ / TETRAHYDROOXAZINE


Mass: 149.145 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C5H11NO4
#4: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#5: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C2H6O2
#6: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#7: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#8: Chemical ChemComp-PGE / TRIETHYLENE GLYCOL


Mass: 150.173 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H14O4
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 439 / Source method: isolated from a natural source / Formula: H2O

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Details

Compound detailsENGINEERED RESIDUE IN CHAIN A, GLN 103 TO HIS ENGINEERED RESIDUE IN CHAIN A, THR 127 TO VAL ...ENGINEERED RESIDUE IN CHAIN A, GLN 103 TO HIS ENGINEERED RESIDUE IN CHAIN A, THR 127 TO VAL ENGINEERED RESIDUE IN CHAIN A, LYS 153 TO ALA ENGINEERED RESIDUE IN CHAIN A, LYS 164 TO ALA ENGINEERED RESIDUE IN CHAIN A, ARG 191 TO TYR ENGINEERED RESIDUE IN CHAIN A, GLY 235 TO PRO ENGINEERED RESIDUE IN CHAIN A, ASN 366 TO PHE ENGINEERED RESIDUE IN CHAIN A, GLU 393 TO SER ENGINEERED RESIDUE IN CHAIN B, GLN 103 TO HIS ENGINEERED RESIDUE IN CHAIN B, THR 127 TO VAL ENGINEERED RESIDUE IN CHAIN B, LYS 153 TO ALA ENGINEERED RESIDUE IN CHAIN B, LYS 164 TO ALA ENGINEERED RESIDUE IN CHAIN B, ARG 191 TO TYR ENGINEERED RESIDUE IN CHAIN B, GLY 235 TO PRO ENGINEERED RESIDUE IN CHAIN B, ASN 366 TO PHE ENGINEERED RESIDUE IN CHAIN B, GLU 393 TO SER
Sequence detailsSEQUENCE IN DATABASE IS SEQUENCE 2 FROM PATENT US 6815192, WHICH IS FOR A XYLOGLUCANASE-BETA- ...SEQUENCE IN DATABASE IS SEQUENCE 2 FROM PATENT US 6815192, WHICH IS FOR A XYLOGLUCANASE-BETA-MANNANASE (CEL44C-MAN26A), AND THIS STRUCTURE IS FOR THE XYLOGLUCANASE PORTION. THE CONFLICTS WITH UNIPROT ENTRY Q1A2D0 LISTED BELOW WHICH ARE NOT DUE TO ENGINEERED MUTATIONS MAY REPRESENT NATURAL VARIATIONS BETWEEN DIFFERENT STRAINS. THE SEQUENCE FOR THIS STRUCTURE IS PUBLISHED IN PATENT US 6815192, AND GENBANK ENTRY AAW12876.1.

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 2.8 Å3/Da / Density % sol: 57 % / Description: NONE
Crystal growDetails: 25% (W/V) PEG 3350, 0.2M LITHIUM SULPHATE, 0.1M BIS TRIS PH 6.5

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Data collection

DiffractionMean temperature: 120 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I02 / Wavelength: 0.9795
DetectorType: ADSC CCD / Detector: CCD / Date: Oct 7, 2010
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.25→80.01 Å / Num. obs: 62986 / % possible obs: 98.5 % / Observed criterion σ(I): 2 / Redundancy: 8.1 % / Biso Wilson estimate: 35.2 Å2 / Rmerge(I) obs: 0.1 / Net I/σ(I): 14.9
Reflection shellResolution: 2.25→2.37 Å / Redundancy: 5.4 % / Rmerge(I) obs: 0.56 / Mean I/σ(I) obs: 2.7 / % possible all: 92.5

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Processing

Software
NameVersionClassification
REFMAC5.6.0086refinement
XDSdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: APO STRUCTURE, PDB ENTRY 2YKK

2ykk


Resolution: 2.25→106.68 Å / Cor.coef. Fo:Fc: 0.941 / Cor.coef. Fo:Fc free: 0.902 / SU B: 6.396 / SU ML: 0.158 / Cross valid method: THROUGHOUT / ESU R: 0.263 / ESU R Free: 0.226 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 1-6, 442 AND 518-524 IN CHAIN A ARE DISORDERED. RESIDUES 1-7, 442-445 AND 518-524 IN CHAIN B ARE DISORDERED.
RfactorNum. reflection% reflectionSelection details
Rfree0.25948 3188 5.1 %RANDOM
Rwork0.19675 ---
obs0.19988 59645 98.24 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 29.756 Å2
Baniso -1Baniso -2Baniso -3
1-1 Å20.5 Å20 Å2
2--1 Å20 Å2
3----1.51 Å2
Refinement stepCycle: LAST / Resolution: 2.25→106.68 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7938 0 128 439 8505
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.020.0228313
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.8021.94911291
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.01151026
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.31824.831385
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.084151315
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.641531
X-RAY DIFFRACTIONr_chiral_restr0.120.21215
X-RAY DIFFRACTIONr_gen_planes_refined0.010.0216345
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.248→2.307 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.372 205 -
Rwork0.267 3944 -
obs--89.34 %

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