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- PDB-1dog: REFINED STRUCTURE FOR THE COMPLEX OF 1-DEOXYNOJIRIMYCIN WITH GLUC... -

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Basic information

Entry
Database: PDB / ID: 1dog
TitleREFINED STRUCTURE FOR THE COMPLEX OF 1-DEOXYNOJIRIMYCIN WITH GLUCOAMYLASE FROM (ASPERGILLUS AWAMORI) VAR. X100 TO 2.4 ANGSTROMS RESOLUTION
ComponentsGLUCOAMYLASE-471
KeywordsHYDROLASE
Function / homology
Function and homology information


glucan 1,4-alpha-glucosidase / glucan 1,4-alpha-glucosidase activity / starch binding / polysaccharide catabolic process
Similarity search - Function
Glucoamylase, CBM20 domain / Glucoamylase, starch-binding / Glucoamylase active site region signature. / Glucoamylase / Glycosyl hydrolases family 15 / GH15-like domain / CBM20 (carbohydrate binding type-20) domain profile. / Starch binding domain / Carbohydrate binding module family 20 / Starch binding domain ...Glucoamylase, CBM20 domain / Glucoamylase, starch-binding / Glucoamylase active site region signature. / Glucoamylase / Glycosyl hydrolases family 15 / GH15-like domain / CBM20 (carbohydrate binding type-20) domain profile. / Starch binding domain / Carbohydrate binding module family 20 / Starch binding domain / Carbohydrate-binding-like fold / Glycosyltransferase - #10 / Six-hairpin glycosidase-like superfamily / Six-hairpin glycosidase superfamily / Glycosyltransferase / Alpha/alpha barrel / Immunoglobulin-like fold / Mainly Alpha
Similarity search - Domain/homology
Glucoamylase I / alpha-D-mannopyranose / 1-DEOXYNOJIRIMYCIN / Glucoamylase
Similarity search - Component
Biological speciesAspergillus awamori (mold)
MethodX-RAY DIFFRACTION / Resolution: 2.3 Å
AuthorsHarris, E. / Aleshin, A. / Firsov, L. / Honzatko, R.B.
Citation
Journal: Biochemistry / Year: 1993
Title: Refined structure for the complex of 1-deoxynojirimycin with glucoamylase from Aspergillus awamori var. X100 to 2.4-A resolution.
Authors: Harris, E.M. / Aleshin, A.E. / Firsov, L.M. / Honzatko, R.B.
#1: Journal: J.Biol.Chem. / Year: 1992
Title: Crystal Structure of Glucoamylase from Aspergillus Awamori Var. X100 to 2.2-A Resolution
Authors: Aleshin, A. / Golubev, A. / Firsov, L.M. / Honzatko, R.B.
History
DepositionJan 12, 1993Processing site: BNL
Revision 1.0Jan 31, 1994Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Non-polymer description / Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / struct_asym / struct_conn / struct_ref_seq_dif / 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_seq_id / _atom_site.label_asym_id / _atom_site.label_entity_id / _atom_site.pdbx_PDB_ins_code / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_ptnr1_PDB_ins_code / _struct_conn.pdbx_ptnr2_PDB_ins_code / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: GLUCOAMYLASE-471
hetero molecules


Theoretical massNumber of molelcules
Total (without water)54,88715
Polymers50,4511
Non-polymers4,43614
Water10,899605
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)116.600, 103.600, 48.300
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Atom site foot note1: A CIS-PEPTIDE LINK EXISTS BETWEEN GLY 23 AND ALA 24.
2: RESIDUES ASN 171 AND ASN 395 ARE SITES OF N-GLYCOSYLATION.
3: RESIDUES SER 443, SER 444, THR 452, SER 453, SER 455, THR 457, SER 459, SER 460, THR 462 AND THR 464 ARE SITES OF O-GLYCOSYLATION.
4: RESIDUES PRO 46 AND PRO 123 ARE CIS PROLINES. / 5: WATERS 1200, 1201 AND 1202 WERE CO-REFINED WITH NOJ 481.

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Components

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Protein , 1 types, 1 molecules A

#1: Protein GLUCOAMYLASE-471


Mass: 50450.730 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Aspergillus awamori (mold)
References: UniProt: P23176, UniProt: P69327*PLUS, glucan 1,4-alpha-glucosidase

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Sugars , 3 types, 12 molecules

#2: Polysaccharide alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-2DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_d2-e1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{[(2+1)][a-D-Manp]{}}}}}}LINUCSPDB-CARE
#3: Polysaccharide alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1397.245 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-2DManpa1-2DManpa1-3[DManpa1-3DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,8,7/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3-3-3/a4-b1_b4-c1_c3-d1_c6-g1_d2-e1_e2-f1_g3-h1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{[(2+1)][a-D-Manp]{[(2+1)][a-D-Manp]{}}}[(6+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}}}}}}LINUCSPDB-CARE
#4: Sugar
ChemComp-MAN / alpha-D-mannopyranose / Mannose


Type: D-saccharide, alpha linking / Mass: 180.156 Da / Num. of mol.: 10
Source method: isolated from a genetically manipulated source
Formula: C6H12O6
IdentifierTypeProgram
DManpaCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
a-D-mannopyranoseCOMMON NAMEGMML 1.0
a-D-ManpIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
ManSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 2 types, 607 molecules

#5: Chemical ChemComp-NOJ / 1-DEOXYNOJIRIMYCIN / MORANOLINE / 1-Deoxynojirimycin


Mass: 163.172 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H13NO4 / Comment: inhibitor*YM
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 605 / Source method: isolated from a natural source / Formula: H2O

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Details

Compound detailsACTIVE SITE: (SEE TABLE II OF MANUSCRIPT AND THE DISCUSSION CONCERNING THE CATALYTIC MECHANISM) ...ACTIVE SITE: (SEE TABLE II OF MANUSCRIPT AND THE DISCUSSION CONCERNING THE CATALYTIC MECHANISM) RESIDUES THAT BIND TO 1-DEOXYNOJIRIMYCIN AT ITS PRINCIPAL SITE ARE ASP 55 OD1, ASP 55 OD2, ARG 305 NH1, CARBONYL 177, ARG 54 NE, AND ARG 54 NH2. GLU 179 IS THE CATALYTIC ACID AND RESIDUE GLU 400 IS THE CATALYTIC BASE. WATER 1201 IS THE NUCLEOPHILE.
Nonpolymer detailsTHERE ARE SOME CLOSE CONTACTS BETWEEN WATERS AND THE DEOXYNOJIRIMYCIN MOLECULE WHICH ARE THE RESULT ...THERE ARE SOME CLOSE CONTACTS BETWEEN WATERS AND THE DEOXYNOJIRIMYCIN MOLECULE WHICH ARE THE RESULT OF THE CO-REFINEMENT OF AN INHIBITOR MOLECULE AT LESS THAN FULL OCCUPANCY ALONG WITH SOLVENT MOLECULES WHICH ARE PRESENT IN THE ABSENCE OF THE INHIBITOR. THE PAPER CITED ON JRNL RECORDS ABOVE DISCUSSES THIS BRIEFLY IN THE METHODS SECTION.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.89 Å3/Da / Density % sol: 57.44 %
Crystal grow
*PLUS
pH: 5.95 / Method: vapor diffusion
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
115 mg/mlprotein1drop
250 mMpotassium phosphate1drop
313 %(w/v)PEG60001drop
450 mMphosphate1reservoir
520 %(w/v)PEG60001reservoir

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1
Reflection
*PLUS
Highest resolution: 2.3 Å / Num. all: 26797 / Num. obs: 20987 / Num. measured all: 52047 / Rmerge(I) obs: 0.033

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Processing

SoftwareName: PROLSQ / Classification: refinement
RefinementResolution: 2.3→10 Å / Rfactor obs: 0.119 / σ(F): 1
Refinement stepCycle: LAST / Resolution: 2.3→10 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3562 0 287 605 4454
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONp_bond_d0.0120.02
X-RAY DIFFRACTIONp_angle_d0.030.03
X-RAY DIFFRACTIONp_angle_deg
X-RAY DIFFRACTIONp_planar_d0.040.05
X-RAY DIFFRACTIONp_hb_or_metal_coord
X-RAY DIFFRACTIONp_mcbond_it0.6051
X-RAY DIFFRACTIONp_mcangle_it1.0371.5
X-RAY DIFFRACTIONp_scbond_it1.8652
X-RAY DIFFRACTIONp_scangle_it2.8173
X-RAY DIFFRACTIONp_plane_restr0.0120.02
X-RAY DIFFRACTIONp_chiral_restr0.1370.15
X-RAY DIFFRACTIONp_singtor_nbd0.2250.25
X-RAY DIFFRACTIONp_multtor_nbd0.1590.25
X-RAY DIFFRACTIONp_xhyhbond_nbd0.2010.25
X-RAY DIFFRACTIONp_xyhbond_nbd
X-RAY DIFFRACTIONp_planar_tor2.23
X-RAY DIFFRACTIONp_staggered_tor14.210
X-RAY DIFFRACTIONp_orthonormal_tor28.520
X-RAY DIFFRACTIONp_transverse_tor
X-RAY DIFFRACTIONp_special_tor
Software
*PLUS
Name: PROLSQ / Classification: refinement
Refinement
*PLUS
Num. reflection obs: 20387 / Rfactor obs: 0.119
Solvent computation
*PLUS
Displacement parameters
*PLUS
Biso mean: 10.02 Å2

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