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- PDB-3l6o: Crystal Structure of Phosphate bound apo Glyceraldehyde-3-phospha... -

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Basic information

Entry
Database: PDB / ID: 3l6o
TitleCrystal Structure of Phosphate bound apo Glyceraldehyde-3-phosphate dehydrogenase 1 from MRSA252 at 2.2 Angstrom resolution
ComponentsGlyceraldehyde-3-phosphate dehydrogenase 1Glyceraldehyde 3-phosphate dehydrogenase
KeywordsOXIDOREDUCTASE / glycolysis / NAD
Function / homology
Function and homology information


glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) / glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity / glycolytic process / glucose metabolic process / NAD binding / NADP binding / cytoplasm
Similarity search - Function
Glyceraldehyde-3-phosphate dehydrogenase, type I / Glyceraldehyde 3-phosphate dehydrogenase, active site / Glyceraldehyde 3-phosphate dehydrogenase active site. / Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain / Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain / Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain / Glyceraldehyde/Erythrose phosphate dehydrogenase family / Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain / Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain / Dihydrodipicolinate Reductase; domain 2 ...Glyceraldehyde-3-phosphate dehydrogenase, type I / Glyceraldehyde 3-phosphate dehydrogenase, active site / Glyceraldehyde 3-phosphate dehydrogenase active site. / Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain / Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain / Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain / Glyceraldehyde/Erythrose phosphate dehydrogenase family / Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain / Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain / Dihydrodipicolinate Reductase; domain 2 / Dihydrodipicolinate Reductase; domain 2 / NAD(P)-binding Rossmann-like Domain / NAD(P)-binding domain superfamily / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
PHOSPHATE ION / Glyceraldehyde-3-phosphate dehydrogenase 1
Similarity search - Component
Biological speciesStaphylococcus aureus (bacteria)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.2 Å
AuthorsMukherjee, S. / Dutta, D. / Saha, B. / Das, A.K.
CitationJournal: J.Mol.Biol. / Year: 2010
Title: Crystal structure of glyceraldehyde-3-phosphate dehydrogenase 1 from methicillin-resistant Staphylococcus aureus MRSA252 provides novel insights into substrate binding and catalytic mechanism.
Authors: Mukherjee, S. / Dutta, D. / Saha, B. / Das, A.K.
History
DepositionDec 23, 2009Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Aug 18, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Dec 11, 2013Group: Database references
Revision 1.3Nov 1, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
Q: Glyceraldehyde-3-phosphate dehydrogenase 1
P: Glyceraldehyde-3-phosphate dehydrogenase 1
R: Glyceraldehyde-3-phosphate dehydrogenase 1
O: Glyceraldehyde-3-phosphate dehydrogenase 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)145,6638
Polymers145,2834
Non-polymers3804
Water2,450136
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15930 Å2
ΔGint-54 kcal/mol
Surface area44510 Å2
MethodPISA
Unit cell
Length a, b, c (Å)66.955, 93.683, 89.054
Angle α, β, γ (deg.)90.000, 106.840, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11Q
21P
31R
41O

NCS domain segments:

Ens-ID: 1 / Refine code: 2

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ALAALAPHEPHEQA2 - 182 - 18
21ALAALAPHEPHEPB2 - 182 - 18
31ALAALAPHEPHERC2 - 182 - 18
41ALAALAPHEPHEOD2 - 182 - 18
12VALVALMETMETQA30 - 5030 - 50
22VALVALMETMETPB30 - 5030 - 50
32VALVALMETMETRC30 - 5030 - 50
42VALVALMETMETOD30 - 5030 - 50
13GLYGLYVALVALQA56 - 6056 - 60
23GLYGLYVALVALPB56 - 6056 - 60
33GLYGLYVALVALRC56 - 6056 - 60
43GLYGLYVALVALOD56 - 6056 - 60
14LYSLYSSERSERQA70 - 7470 - 74
24LYSLYSSERSERPB70 - 7470 - 74
34LYSLYSSERSERRC70 - 7470 - 74
44LYSLYSSERSEROD70 - 7470 - 74
15SERSERSERSERQA81 - 21081 - 210
25SERSERSERSERPB81 - 21081 - 210
35SERSERSERSERRC81 - 21081 - 210
45SERSERSERSEROD81 - 21081 - 210
16GLYGLYGLUGLUQA218 - 333218 - 333
26GLYGLYGLUGLUPB218 - 333218 - 333
36GLYGLYGLUGLURC218 - 333218 - 333
46GLYGLYGLUGLUOD218 - 333218 - 333

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Components

#1: Protein
Glyceraldehyde-3-phosphate dehydrogenase 1 / Glyceraldehyde 3-phosphate dehydrogenase / GAPDH 1


Mass: 36320.762 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria) / Strain: MRSA252 / Gene: gap, gap1, gapA, gapA1, SAR0828 / Plasmid: pQE30 / Production host: Escherichia coli (E. coli) / Strain (production host): M15
References: UniProt: Q6GIL8, glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
#2: Chemical
ChemComp-PO4 / PHOSPHATE ION / Phosphate


Mass: 94.971 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: PO4
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 136 / Source method: isolated from a natural source / Formula: H2O

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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: 1.84 Å3/Da / Density % sol: 33.15 % / Mosaicity: 1.708 °
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8.7
Details: 0.1M Tris-HCl pH 8.7, 32% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.5418 Å
DetectorType: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Dec 9, 2009 / Details: Varimax mirrors
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2.2→33.34 Å / Num. obs: 53348 / % possible obs: 99.7 % / Redundancy: 3.61 % / Biso Wilson estimate: 36.1 Å2 / Rmerge(I) obs: 0.088 / Χ2: 0.96 / Net I/σ(I): 6.8 / Scaling rejects: 1454
Reflection shellResolution: 2.2→2.28 Å / Redundancy: 3.33 % / Rmerge(I) obs: 0.428 / Mean I/σ(I) obs: 2.3 / Num. measured all: 17409 / Num. unique all: 5203 / Χ2: 1.15 / % possible all: 97.3

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Processing

Software
NameVersionClassificationNB
d*TREK9.8Ldata scaling
REFMAC5.5.0095refinement
PDB_EXTRACT3.005data extraction
StructureStudiodata collection
d*TREKdata reduction
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3H48

3h48
PDB Unreleased entry


Resolution: 2.2→20 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.93 / Occupancy max: 1 / Occupancy min: 1 / SU B: 22.775 / SU ML: 0.258 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.504 / ESU R Free: 0.261 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.258 2706 5.1 %RANDOM
Rwork0.216 ---
obs0.218 53279 99.67 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso max: 102.77 Å2 / Biso mean: 63.605 Å2 / Biso min: 27.72 Å2
Baniso -1Baniso -2Baniso -3
1-0.78 Å20 Å2-0.32 Å2
2--1.08 Å20 Å2
3----2.05 Å2
Refinement stepCycle: LAST / Resolution: 2.2→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10116 0 20 136 10272
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0140.02210268
X-RAY DIFFRACTIONr_angle_refined_deg1.4691.95913913
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.68851331
X-RAY DIFFRACTIONr_dihedral_angle_2_deg38.55525.391460
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.015151770
X-RAY DIFFRACTIONr_dihedral_angle_4_deg23.6721556
X-RAY DIFFRACTIONr_chiral_restr0.0950.21630
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.027684
X-RAY DIFFRACTIONr_mcbond_it0.7741.56591
X-RAY DIFFRACTIONr_mcangle_it1.5072.510596
X-RAY DIFFRACTIONr_scbond_it3.92953677
X-RAY DIFFRACTIONr_scangle_it6.588103317
Refine LS restraints NCS

Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Dom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1Q1176TIGHT POSITIONAL0.070.05
2P1176TIGHT POSITIONAL0.060.05
3R1176TIGHT POSITIONAL0.070.05
4O1176TIGHT POSITIONAL0.070.05
1Q1052MEDIUM POSITIONAL0.070.5
2P1052MEDIUM POSITIONAL0.070.5
3R1052MEDIUM POSITIONAL0.080.5
4O1052MEDIUM POSITIONAL0.070.5
1Q1176TIGHT THERMAL0.651.5
2P1176TIGHT THERMAL0.591.5
3R1176TIGHT THERMAL0.691.5
4O1176TIGHT THERMAL0.611.5
1Q1052MEDIUM THERMAL0.932.5
2P1052MEDIUM THERMAL0.972.5
3R1052MEDIUM THERMAL0.962.5
4O1052MEDIUM THERMAL0.992.5
LS refinement shellResolution: 2.2→2.256 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.367 194 -
Rwork0.323 3602 -
all-3796 -
obs--96.35 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
11.02950.24930.08091.0590.30310.2027-0.0140.16270.2128-0.04790.0125-0.0466-0.0224-0.0010.00150.0163-0.00070.0270.02670.03510.106722.368-0.78117.3002
21.5645-0.4503-0.40390.6238-0.31470.61440.0069-0.07510.10940.02540.05110.02090.0369-0.0564-0.0580.0502-0.01340.02030.035-0.01520.0323-7.9275-7.431533.9379
30.36060.32080.26511.0005-0.16441.57880.06860.0446-0.0947-0.01680.0081-0.0310.2409-0.0785-0.07670.0448-0.007-0.01020.0228-0.02310.05534.0469-34.54979.3366
41.38430.29480.1970.34610.09411.83770.0133-0.2181-0.28860.0917-0.0743-0.1155-0.01360.23250.0610.0338-0.015-0.01080.07720.06870.100127.7969-20.629439.5489
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1Q1 - 334
2X-RAY DIFFRACTION2P1 - 334
3X-RAY DIFFRACTION3R1 - 334
4X-RAY DIFFRACTION4O1 - 333

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