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- PDB-9kei: human glyoxalase I (with C-ter His tag) in complex with licochalc... -

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Basic information

Entry
Database: PDB / ID: 9kei
Titlehuman glyoxalase I (with C-ter His tag) in complex with licochalcone B, form 4
ComponentsLactoylglutathione lyase
KeywordsLYASE / glyoxalase i / zinc metalloenzyme
Function / homology
Function and homology information


lactoylglutathione lyase / lactoylglutathione lyase activity / methylglyoxal metabolic process / Pyruvate metabolism / glutathione metabolic process / osteoclast differentiation / carbohydrate metabolic process / regulation of transcription by RNA polymerase II / negative regulation of apoptotic process / extracellular exosome ...lactoylglutathione lyase / lactoylglutathione lyase activity / methylglyoxal metabolic process / Pyruvate metabolism / glutathione metabolic process / osteoclast differentiation / carbohydrate metabolic process / regulation of transcription by RNA polymerase II / negative regulation of apoptotic process / extracellular exosome / zinc ion binding / nucleoplasm / plasma membrane / cytoplasm / cytosol
Similarity search - Function
Glyoxalase I signature 2. / Glyoxalase I / Glyoxalase I, conserved site / Glyoxalase I signature 1. / Glyoxalase/fosfomycin resistance/dioxygenase domain / Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily / Vicinal oxygen chelate (VOC) domain / Vicinal oxygen chelate (VOC) domain profile. / Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Similarity search - Domain/homology
: / BETA-MERCAPTOETHANOL / TRIETHYLENE GLYCOL / Lactoylglutathione lyase
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.81 Å
AuthorsAndo, K. / Yokoyama, H.
Funding support Japan, 1items
OrganizationGrant numberCountry
Japan Society for the Promotion of Science (JSPS)22K06554 Japan
CitationJournal: To Be Published
Title: Crystal structures of glyoxalase I complexes with nature-derived inhibitors reveal flexible and multiple binding poses
Authors: Ando, K. / Yokoyama, H.
History
DepositionNov 5, 2024Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Nov 12, 2025Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Lactoylglutathione lyase
B: Lactoylglutathione lyase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)44,8329
Polymers43,7502
Non-polymers1,0827
Water3,207178
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8670 Å2
ΔGint-124 kcal/mol
Surface area15540 Å2
MethodPISA
Unit cell
Length a, b, c (Å)68.874, 66.063, 41.772
Angle α, β, γ (deg.)90.00, 100.01, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein Lactoylglutathione lyase / Aldoketomutase / Glyoxalase I / Glx I / Ketone-aldehyde mutase / Methylglyoxalase / S-D- ...Aldoketomutase / Glyoxalase I / Glx I / Ketone-aldehyde mutase / Methylglyoxalase / S-D-lactoylglutathione methylglyoxal lyase


Mass: 21874.869 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: GLO1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q04760, lactoylglutathione lyase

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Non-polymers , 5 types, 185 molecules

#2: Chemical ChemComp-A1L5R / 1-(4-hydroxyphenyl)-3-[2-methoxy-3,4-bis(oxidanyl)phenyl]prop-2-en-1-one / Licochalcone B


Mass: 286.279 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C16H14O5 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-PGE / TRIETHYLENE GLYCOL


Mass: 150.173 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H14O4
#4: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#5: Chemical ChemComp-BME / BETA-MERCAPTOETHANOL


Mass: 78.133 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6OS
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 178 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY
Has protein modificationN

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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: 2.14 Å3/Da / Density % sol: 42.5 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5.8
Details: 0.2 M Sodium chloride, 0.1 M MES, 25%(w/v) PEG 3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: BL-1A / Wavelength: 1.018 Å
DetectorType: DECTRIS EIGER X 4M / Detector: PIXEL / Date: Jun 26, 2024
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.018 Å / Relative weight: 1
ReflectionResolution: 1.81→19.76 Å / Num. obs: 33704 / % possible obs: 100 % / Redundancy: 3.5 % / CC1/2: 0.958 / Rmerge(I) obs: 0.075 / Net I/σ(I): 19.1
Reflection shellResolution: 1.81→1.84 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.301 / Mean I/σ(I) obs: 4 / Num. unique obs: 1663 / CC1/2: 0.92 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.8.0425refinement
DIALSdata scaling
DIALSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.81→19.76 Å / Cor.coef. Fo:Fc: 0.94 / Cor.coef. Fo:Fc free: 0.905 / SU B: 6.909 / SU ML: 0.097 / Cross valid method: THROUGHOUT / ESU R: 0.138 / ESU R Free: 0.135 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
RfactorNum. reflection% reflectionSelection details
Rfree0.2384 1667 4.9 %RANDOM
Rwork0.1908 ---
obs0.19322 32019 99.91 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 23.862 Å2
Baniso -1Baniso -2Baniso -3
1--0.55 Å2-0 Å20.11 Å2
2---1.62 Å20 Å2
3---2.01 Å2
Refinement stepCycle: 1 / Resolution: 1.81→19.76 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2799 0 68 178 3045
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.0122928
X-RAY DIFFRACTIONr_bond_other_d0.0010.0162742
X-RAY DIFFRACTIONr_angle_refined_deg2.4161.8433940
X-RAY DIFFRACTIONr_angle_other_deg0.8241.7886372
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.4385350
X-RAY DIFFRACTIONr_dihedral_angle_2_deg27.1589.520
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.5910522
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.1290.2412
X-RAY DIFFRACTIONr_gen_planes_refined0.0140.023348
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02628
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_it2.3041.6211406
X-RAY DIFFRACTIONr_mcbond_other2.3041.6251407
X-RAY DIFFRACTIONr_mcangle_it3.1562.8921754
X-RAY DIFFRACTIONr_mcangle_other3.1582.8961755
X-RAY DIFFRACTIONr_scbond_it3.4031.9671522
X-RAY DIFFRACTIONr_scbond_other3.4021.9681523
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other4.9613.4562187
X-RAY DIFFRACTIONr_long_range_B_refined6.34317.523303
X-RAY DIFFRACTIONr_long_range_B_other6.34317.523304
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.81→1.857 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.288 126 -
Rwork0.224 2310 -
obs--100 %
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)
10.77930.03480.06170.858-0.19160.40250.0404-0.0541-0.11710.0316-0.048-0.05920.0041-0.02360.00760.0042-0.0082-0.00510.01970.00110.029320.359510.80943.4194
20.84780.08020.07230.9406-0.17880.33260.022-0.0117-0.007-0.0601-0.00970.0209-0.0256-0.0146-0.01220.0149-0.00260.00620.0294-0.01540.013615.328820.6642-2.8487
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A8 - 183
2X-RAY DIFFRACTION2B8 - 183

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