SAXSdb — 1bh5

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1. Protein Identity and Related Structures Protein Identity & Related Structures

LACTOYLGLUTATHIONE LYASE

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–183 Chain B； UniProt 1–183	Mutation：Q33E, E172Q	ZN ZINC ION × 2 GTX S-HEXYLGLUTATHIONE × 2	X-RAY DIFFRACTION X-ray crystallization conditions：pH 5.8；PROTEIN WAS CRYSTALLISED FROM PEG 2000 MONOMETHLY ETHER 50 MM MES PH 5.8, 0.1M NACL	Resolution 2.20 Å R-free 0.250
2	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 1–183 Chain D； UniProt 1–183	Mutation：Q33E, E172Q	ZN ZINC ION × 2 GTX S-HEXYLGLUTATHIONE × 2	X-RAY DIFFRACTION X-ray crystallization conditions：pH 5.8；PROTEIN WAS CRYSTALLISED FROM PEG 2000 MONOMETHLY ETHER 50 MM MES PH 5.8, 0.1M NACL	Resolution 2.20 Å R-free 0.250

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1BH5	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1FRO HUMAN GLYOXALASE I WITH BENZYL-GLUTATHIONE INHIBITOR Deposited 1997-02-25	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2–184（183 aa） Chain B 2–184（183 aa）	Not recorded	ZN ZINC ION × 2 GSB S-BENZYL-GLUTATHIONE × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.8；pH 5.8	Resolution 2.20 Å R-free 0.234
1FRO HUMAN GLYOXALASE I WITH BENZYL-GLUTATHIONE INHIBITOR Deposited 1997-02-25	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 2–184（183 aa） Chain D 2–184（183 aa）	Not recorded	ZN ZINC ION × 2 GSB S-BENZYL-GLUTATHIONE × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.8；pH 5.8	Resolution 2.20 Å R-free 0.234
1QIN HUMAN GLYOXALASE I COMPLEXED WITH S-(N-HYDROXY-N-P-IODOPHENYLCARBAMOYL) GLUTATHIONE Deposited 1999-06-14	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–183（183 aa） Chain B 1–183（183 aa）	Not recorded	ZN ZINC ION × 2 GIP S-(N-HYDROXY-N-IODOPHENYLCARBAMOYL)GLUTATHIONE × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.8；PROTEIN WAS CRYSTALLISED BY EQILLABRATION AGAINST PEG 2000 MONOMETHLY ETHER, 50 MM MES PH 5.8, 0.1M NACL. HIPC-GSH WAS PRESENT IN THE PROTEIN SOLUTION	Resolution 2.00 Å R-free 0.210
1QIP HUMAN GLYOXALASE I COMPLEXED WITH S-P-NITROBENZYLOXYCARBONYLGLUTATHIONE Deposited 1999-06-14	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–183（183 aa） Chain B 1–183（183 aa）	Not recorded	ZN ZINC ION × 2 GNB S-P-NITROBENZYLOXYCARBONYLGLUTATHIONE × 2 BME BETA-MERCAPTOETHANOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.8；PROTEIN WAS CRYSTALLISED BY EQILLABRATION AGAINST PEG 2000 MONOMETHLY ETHER, 50 MM MES PH 5.8, 0.1M NACL THEN SOAKED IN 10MM NBC-GSH	Resolution 1.72 Å R-free 0.210
1QIP HUMAN GLYOXALASE I COMPLEXED WITH S-P-NITROBENZYLOXYCARBONYLGLUTATHIONE Deposited 1999-06-14	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–183（183 aa） Chain D 1–183（183 aa）	Not recorded	ZN ZINC ION × 2 GNB S-P-NITROBENZYLOXYCARBONYLGLUTATHIONE × 2 BME BETA-MERCAPTOETHANOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.8；PROTEIN WAS CRYSTALLISED BY EQILLABRATION AGAINST PEG 2000 MONOMETHLY ETHER, 50 MM MES PH 5.8, 0.1M NACL THEN SOAKED IN 10MM NBC-GSH	Resolution 1.72 Å R-free 0.210
3VW9 Human Glyoxalase I with an N-hydroxypyridone inhibitor Deposited 2012-08-10	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–184（184 aa） Chain B 1–184（184 aa）	Not recorded	ZN ZINC ION × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 HPJ 1-hydroxy-6-[1-(3-methoxypropyl)-1H-pyrrolo[2,3-b]pyridin-5-yl]-4-phenylpyridin-2(1H)-one × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；25%(w/v) PEG 2000 MME, 10%(v/v) Glycerol, 0.1M Na-HEPES (pH 7.0), vapor diffusion, hanging drop, temperature 293K	Resolution 1.47 Å R-free 0.193
3W0T Human Glyoxalase I with an N-hydroxypyridone derivative inhibitor Deposited 2012-11-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–184（184 aa） Chain B 1–184（184 aa）	Not recorded	ZN ZINC ION × 2 HPU N-[3-(1-hydroxy-6-oxo-4-phenyl-1,6-dihydropyridin-2-yl)phenyl]methanesulfonamide × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；33% (w/v) PEG 2000 MME, 0.1M Na-HEPES (pH 7.0), vapor diffusion, hanging drop, temperature 293K	Resolution 1.35 Å R-free 0.197
3W0T Human Glyoxalase I with an N-hydroxypyridone derivative inhibitor Deposited 2012-11-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–184（184 aa） Chain D 1–184（184 aa）	Not recorded	ZN ZINC ION × 2 HPU N-[3-(1-hydroxy-6-oxo-4-phenyl-1,6-dihydropyridin-2-yl)phenyl]methanesulfonamide × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；33% (w/v) PEG 2000 MME, 0.1M Na-HEPES (pH 7.0), vapor diffusion, hanging drop, temperature 293K	Resolution 1.35 Å R-free 0.197
3W0U human Glyoxalase I with an N-hydroxypyridone inhibitor Deposited 2012-11-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–184（184 aa） Chain B 1–184（184 aa）	Not recorded	ZN ZINC ION × 2 HPW N-[3-(1-Hydroxy-6-oxo-4-phenyl-1,6-dihydro-pyridin-2-yl)-5-methanesulfonylamino-phenyl]-methanesulfonamide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；25% (w/v) PEG 2000 MME, 10%(v/v) Glycerol, 0.1M Na-HEPES (pH 7.0), vapor diffusion, hanging drop, temperature 293K	Resolution 1.70 Å R-free 0.242
7WSZ human glyoxalase I (with C-ter His tag) in glycerol-bound form Deposited 2022-02-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–184（184 aa） Chain B 1–184（184 aa）	Not recorded	ZN ZINC ION × 2 GOL GLYCEROL × 4 BO3 BORIC ACID × 3 IMD IMIDAZOLE × 1 BME BETA-MERCAPTOETHANOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M MIB (sodium malonate, imidazole, and boric acid), 25% PEG1500	Resolution 1.52 Å R-free 0.187
7WT0 human glyoxalase I (with C-ter His tag) in complex with TLSC702 Deposited 2022-02-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–184（184 aa） Chain B 1–184（184 aa）	Not recorded	ZN ZINC ION × 2 5ZO (~{E})-3-(1,3-benzothiazol-2-yl)-4-(4-methoxyphenyl)but-3-enoic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M MgCl2, 0.1 M Bis-Tris, 25% PEG3350	Resolution 2.00 Å R-free 0.222
7WT1 human glyoxalase I (with C-ter His tag) in inhibitor-free form Deposited 2022-02-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–184（184 aa） Chain B 1–184（184 aa）	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M NaCl, 0.1 M MES-NaOH, 25% PEG3350	Resolution 1.85 Å R-free 0.230
7WT2 human glyoxalase I in complex with TLSC702 Deposited 2022-02-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–184（184 aa） Chain B 1–184（184 aa）	Not recorded	ZN ZINC ION × 2 5ZO (~{E})-3-(1,3-benzothiazol-2-yl)-4-(4-methoxyphenyl)but-3-enoic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M NaCl, 0.1 M Bis-Tris, 25% PEG3350	Resolution 2.00 Å R-free 0.228
9KEE human glyoxalase I (with C-ter His tag) in complex with licochalcone B, form 1 Deposited 2024-11-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–184（184 aa） Chain B 1–184（184 aa）	Not recorded	ZN ZINC ION × 2 A1L5R 1-(4-hydroxyphenyl)-3-[2-methoxy-3,4-bis(oxidanyl)phenyl]prop-2-en-1-one × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；0.2 M Sodium chloride, 0.1 M Bis-Tris, 25%(w/v) PEG 3350	Resolution 2.08 Å R-free 0.234
9KEG human glyoxalase I (with C-ter His tag) in complex with licochalcone B, form 2 Deposited 2024-11-05	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–184（184 aa） Chain B 1–184（184 aa）	Not recorded	A1L5R 1-(4-hydroxyphenyl)-3-[2-methoxy-3,4-bis(oxidanyl)phenyl]prop-2-en-1-one × 2 PG4 TETRAETHYLENE GLYCOL × 2 BME BETA-MERCAPTOETHANOL × 3 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.8；293 K；0.2 M Sodium chloride, 0.1 M MES, 25%(w/v) PEG 3350	Resolution 1.80 Å R-free 0.239
9KEH human glyoxalase I (with C-ter His tag) in complex with licochalcone B and GSH, form 3 Deposited 2024-11-05	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–184（184 aa） Chain B 1–184（184 aa）	Not recorded	ZN ZINC ION × 2 A1L5R 1-(4-hydroxyphenyl)-3-[2-methoxy-3,4-bis(oxidanyl)phenyl]prop-2-en-1-one × 2 PG4 TETRAETHYLENE GLYCOL × 2 GSH Glutathione × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；0.2 M Sodium chloride, 0.1 M Bis-Tris, 25%(w/v) PEG 3350	Resolution 1.72 Å R-free 0.193
9KEI human glyoxalase I (with C-ter His tag) in complex with licochalcone B, form 4 Deposited 2024-11-05	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–184（184 aa） Chain B 1–184（184 aa）	Not recorded	A1L5R 1-(4-hydroxyphenyl)-3-[2-methoxy-3,4-bis(oxidanyl)phenyl]prop-2-en-1-one × 2 PGE TRIETHYLENE GLYCOL × 2 ZN ZINC ION × 2 BME BETA-MERCAPTOETHANOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.8；293 K；0.2 M Sodium chloride, 0.1 M MES, 25%(w/v) PEG 3350	Resolution 1.81 Å R-free 0.238
9KEK human glyoxalase I (with C-ter His tag) in complex with piceatannol Deposited 2024-11-05	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–184（184 aa） Chain B 1–184（184 aa）	Not recorded	ZN ZINC ION × 2 PIT PICEATANNOL × 2 PG4 TETRAETHYLENE GLYCOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；0.2 M Sodium chloride, 0.1 M Bis-Tris, 25%(w/v) PEG 3350	Resolution 2.11 Å R-free 0.233
9KEK human glyoxalase I (with C-ter His tag) in complex with piceatannol Deposited 2024-11-05	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–184（184 aa） Chain D 1–184（184 aa）	Not recorded	ZN ZINC ION × 2 PIT PICEATANNOL × 1 PG4 TETRAETHYLENE GLYCOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；0.2 M Sodium chloride, 0.1 M Bis-Tris, 25%(w/v) PEG 3350	Resolution 2.11 Å R-free 0.233

15 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	LGUL_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–183； UniProt 1–183 Author chain B； PDBConstruct 1–183； UniProt 1–183 Author chain C； PDBConstruct 1–183； UniProt 1–183 Author chain D； PDBConstruct 1–183； UniProt 1–183

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1bh5
Deposition date deposition_date	1998-06-13
Structure title title	HUMAN GLYOXALASE I Q33E, E172Q DOUBLE MUTANT
Keywords keywords	LYASE, LACTOYLGLUTATHIONE LYASE, GLYOXALASE I; LYASE
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	31.42 Å
Radius of gyration Rg (electron density) rg_electron	31.02 Å
Forward intensity I(0) i0	108890000.00
Molecular weight molecular_weight	83014.0 kDa
Excluded volume excluded_volume	103860 Å³
Envelope volume envelope_volume	129980 Å³
Hydration-shell volume shell_volume	35741 Å³
Envelope diameter envelope_diameter	119.4 Å
Shell Rg shell_rg	37.12 Å
Envelope Rg envelope_rg	31.28 Å
Shape Rg shape_rg	31.02 Å
Total Rg total_rg	31.56 Å
Total atoms total_atoms	5810
Residues n_residues	718
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	117.1 Å
Rg (real space) rg_real	31.60 Å
Rg uncertainty (real space) rg_real_error	1.19 Å
I(0) (real space) i0_real	1.0890e+08
I(0) uncertainty (real space) i0_real_error	1.6750e+06
Rg (reciprocal space) rg_reciprocal	31.52 Å
I(0) (reciprocal space) i0_reciprocal	108900000.0000
Solution quality estimate total_estimate	0.8069
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	30.4 Å
Skewness Skewness skewness	0.475
Kurtosis Kurtosis kurtosis	-0.377
Angular range angular_range	— – 0.2500 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	40010000.0000
Real-space data points n_real_points	51
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.562; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.800; Smooth: 0.998

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	LACTOYLGLUTATHIONE LYASE
Molecular weight formula_weight	20672.5 kDa
EC 编号 ec_number	4.4.1.5
Mutation mutation	Q33E, E172Q
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	6317

AEPQPPSGGLTDEAALSCCSDADPSTKDFLLQETMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIQILNPNKMATLM

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 non-polymer

Description description	S-HEXYLGLUTATHIONE
Molecular weight formula_weight	392.5 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	507

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1bh5a_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.32 — Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Superfamily Superfamily superfamily	d.32.1 — Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Family Family family	d.32.1.1 — Glyoxalase I (lactoylglutathione lyase)

Domain ID domain_id	d1bh5b_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.32 — Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Superfamily Superfamily superfamily	d.32.1 — Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Family Family family	d.32.1.1 — Glyoxalase I (lactoylglutathione lyase)

Domain ID domain_id	d1bh5c_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.32 — Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Superfamily Superfamily superfamily	d.32.1 — Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Family Family family	d.32.1.1 — Glyoxalase I (lactoylglutathione lyase)

Domain ID domain_id	d1bh5d_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.32 — Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Superfamily Superfamily superfamily	d.32.1 — Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Family Family family	d.32.1.1 — Glyoxalase I (lactoylglutathione lyase)

CATH v4.4 (4 domains)

Domain ID domain_id	1bh5A00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	180 — 2,3-Dihydroxybiphenyl 1,2-Dioxygenase; domain 1
Homologous superfamily homologous superfamily	10 — 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1

Domain ID domain_id	1bh5B00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	180 — 2,3-Dihydroxybiphenyl 1,2-Dioxygenase; domain 1
Homologous superfamily homologous superfamily	10 — 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1

Domain ID domain_id	1bh5C00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	180 — 2,3-Dihydroxybiphenyl 1,2-Dioxygenase; domain 1
Homologous superfamily homologous superfamily	10 — 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1

Domain ID domain_id	1bh5D00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	180 — 2,3-Dihydroxybiphenyl 1,2-Dioxygenase; domain 1
Homologous superfamily homologous superfamily	10 — 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1

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8. Citations (1)

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Unit-cell length a length_a	67.280 Å
Unit-cell length b length_b	67.280 Å
Unit-cell length c length_c	164.730 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	16

Space group space_group	P 41
Space-group number int_tables_number	76
Crystal system crystal_system	—

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.1900
R_work r_work	0.1800
R_free r_free	0.2500

fit	/app/data/saxs_computation/bh/1bh5/1bh5.fit
pddf	/app/data/pr_computation/bh/1bh5/1bh5.pr.out
profile	/app/data/saxs_computation/bh/1bh5/1bh5.dat

HUMAN GLYOXALASE I Q33E, E172Q DOUBLE MUTANT

1. Protein Identity and Related Structures Protein Identity & Related Structures

LACTOYLGLUTATHIONE LYASE

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction