3zr4

STRUCTURAL EVIDENCE FOR AMMONIA TUNNELING ACROSS THE (BETA-ALPHA)8 BARREL OF THE IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE BIENZYME COMPLEX

Method: X-RAY DIFFRACTION D_max: 114.0 Å Quality: EXCELLENT

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

IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF

THERMOTOGA MARITIMA

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–253	Not recorded	IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH × 1 （Q9X0C8） GOL GLYCEROL × 3 GLN GLUTAMINE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.41 Å R-free 0.258
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 1–253	Not recorded	IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH × 1 （Q9X0C8） GOL GLYCEROL × 2 GLN GLUTAMINE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.41 Å R-free 0.258
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain E； UniProt 1–253	Not recorded	IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH × 1 （Q9X0C8） GOL GLYCEROL × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.41 Å R-free 0.258

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 3ZR4	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1GPW Structural evidence for ammonia tunneling across the (beta/alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex. Deposited 2001-11-12	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–253（253 aa）	Mutation：YES	PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；PROTEIN SOLUTION: 10 MM TRIS (PH 8.0), 1 MM DTT, 1 MM EDTA, 28.8 MG/ML PROTEIN COMPLEX. PRECIPITATE SOLUTION: 15 %[W/V] PEG-8000, 0.9 M AMMONIUM NITRATE, 0.1 M HEPES/HCL (PH 8.5), 10 MM DTT, 5% [V/V] MPD	Resolution 2.40 Å R-free 0.290
1GPW Structural evidence for ammonia tunneling across the (beta/alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex. Deposited 2001-11-12	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–253（253 aa）	Mutation：YES	PO4 PHOSPHATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；PROTEIN SOLUTION: 10 MM TRIS (PH 8.0), 1 MM DTT, 1 MM EDTA, 28.8 MG/ML PROTEIN COMPLEX. PRECIPITATE SOLUTION: 15 %[W/V] PEG-8000, 0.9 M AMMONIUM NITRATE, 0.1 M HEPES/HCL (PH 8.5), 10 MM DTT, 5% [V/V] MPD	Resolution 2.40 Å R-free 0.290
1GPW Structural evidence for ammonia tunneling across the (beta/alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex. Deposited 2001-11-12	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 1–253（253 aa）	Mutation：YES	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；PROTEIN SOLUTION: 10 MM TRIS (PH 8.0), 1 MM DTT, 1 MM EDTA, 28.8 MG/ML PROTEIN COMPLEX. PRECIPITATE SOLUTION: 15 %[W/V] PEG-8000, 0.9 M AMMONIUM NITRATE, 0.1 M HEPES/HCL (PH 8.5), 10 MM DTT, 5% [V/V] MPD	Resolution 2.40 Å R-free 0.290
1THF CYCLASE SUBUNIT OF IMIDAZOLEGLYCEROLPHOSPHATE SYNTHASE FROM THERMOTOGA MARITIMA Deposited 1998-09-17	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain D 1–253（253 aa） Fragment：CYCLASE SUBUNIT	Not recorded	PO4 PHOSPHATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.8；pH 4.80	Resolution 1.45 Å R-free 0.214
1VH7 Crystal structure of a cyclase subunit of imidazolglycerolphosphate synthase Deposited 2003-12-01	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–253（252 aa）	Not recorded	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.90 Å R-free 0.224
2A0N Crystal structure of Imidazole glycerol phosphate synthase subunit hisF (EC 4.1.3.-) (tm1036) from Thermotoga maritima at 1.64 A resolution Deposited 2005-06-16	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–253（253 aa）	Not recorded	IOD IODIDE ION × 7 PO4 PHOSPHATE ION × 1 UNL UNKNOWN LIGAND × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP, NANODROP；pH 6.9；273 K；0.2None Nal, 20.0% PEG-3350, No Buffer, pH 6.9, VAPOR DIFFUSION, SITTING DROP, NANODROP, temperature 273K	Resolution 1.64 Å R-free 0.192
2LLE Computational design of an eight-stranded (beta/alpha)-barrel from fragments of different folds Deposited 2011-11-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 103–247（145 aa）	Mutation：R4I, D78G, I95L, L201A,V213G	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.5；313 K；Ionic strength (raw mmCIF value) 350；Pressure ambient NMR sample composition 0.5 mM [U-100% 15N] CheYHisF-sfr_RM, 50 mM potassium phosphate, 300 mM potassium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] CheYHisF-sfr_RM, 50 mM potassium phosphate, 300 mM potassium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2W6R Crystal structure of an artificial (ba)8-barrel protein designed from identical half barrels Deposited 2008-12-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 123–245（123 aa） Fragment：RESIDUES 123-245 AND 123-253 Chain A 123–253（131 aa） Fragment：RESIDUES 123-245 AND 123-253	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；0.1 M TRIS-HCL PH 8.0, 12% W/V PEG 8000	Resolution 2.10 Å R-free 0.285
2WJZ Crystal structure of (HisH) K181A Y138A mutant of imidazoleglycerolphosphate synthase (HisH HisF) which displays constitutive glutaminase activity Deposited 2009-06-02	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–253（253 aa）	Not recorded	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；PEG8K 10-12%, 100 MM HEPES PH = 8.5 22.5MM NH4NO3 / NH4AC 5% (V/V) MPD 10 MM DTT 20 MM L-GLN PROT. CONC.= 12 MG/ML	Resolution 2.60 Å R-free 0.218
2WJZ Crystal structure of (HisH) K181A Y138A mutant of imidazoleglycerolphosphate synthase (HisH HisF) which displays constitutive glutaminase activity Deposited 2009-06-02	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 1–253（253 aa）	Not recorded	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；PEG8K 10-12%, 100 MM HEPES PH = 8.5 22.5MM NH4NO3 / NH4AC 5% (V/V) MPD 10 MM DTT 20 MM L-GLN PROT. CONC.= 12 MG/ML	Resolution 2.60 Å R-free 0.218
2WJZ Crystal structure of (HisH) K181A Y138A mutant of imidazoleglycerolphosphate synthase (HisH HisF) which displays constitutive glutaminase activity Deposited 2009-06-02	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–253（253 aa）	Not recorded	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；PEG8K 10-12%, 100 MM HEPES PH = 8.5 22.5MM NH4NO3 / NH4AC 5% (V/V) MPD 10 MM DTT 20 MM L-GLN PROT. CONC.= 12 MG/ML	Resolution 2.60 Å R-free 0.218
3OG3 Crystal structure of an artificial thermostable (BA)8-barrel protein from identical half barrels Deposited 2010-08-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 123–219（97 aa） Chain A 99–219（121 aa） Chain A 99–122（24 aa）	Mutation：A3R, Y22H, Y143H Mutation：A3R, Y22H, Y143H Mutation：A3R, Y22H, Y143H	SO4 SULFATE ION × 2 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.2 M ammonium sulfate, 18% PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.08 Å R-free 0.196
4EWN Structure of HisF-D130V+D176V with bound rCdRP Deposited 2012-04-27	Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 1–253（253 aa）	Mutation：D130V-D176V	0VR 1-(O-carboxy-phenylamino)-1-deoxy-D-ribulose-5-phosphate × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.90 Å R-free 0.236
4FX7 Structure of Sym2 D9V+D55V+D130V+D176V Deposited 2012-07-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 123–219（97 aa） Chain A 99–219（121 aa） Chain A 99–122（24 aa）	Mutation：A3R, D9V, Y22H, D55V, D130V, Y143H, D176V Mutation：A3R, D9V, Y22H, D55V, D130V, Y143H, D176V Mutation：A3R, D9V, Y22H, D55V, D130V, Y143H, D176V	PI HYDROGENPHOSPHATE ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.08 Å R-free 0.233
4FX7 Structure of Sym2 D9V+D55V+D130V+D176V Deposited 2012-07-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 123–219（97 aa） Chain B 99–219（121 aa） Chain B 99–122（24 aa）	Mutation：A3R, D9V, Y22H, D55V, D130V, Y143H, D176V Mutation：A3R, D9V, Y22H, D55V, D130V, Y143H, D176V Mutation：A3R, D9V, Y22H, D55V, D130V, Y143H, D176V	PI HYDROGENPHOSPHATE ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.08 Å R-free 0.233
4FX7 Structure of Sym2 D9V+D55V+D130V+D176V Deposited 2012-07-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 123–219（97 aa） Chain C 99–219（121 aa） Chain C 99–122（24 aa）	Mutation：A3R, D9V, Y22H, D55V, D130V, Y143H, D176V Mutation：A3R, D9V, Y22H, D55V, D130V, Y143H, D176V Mutation：A3R, D9V, Y22H, D55V, D130V, Y143H, D176V	PI HYDROGENPHOSPHATE ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.08 Å R-free 0.233
4FX7 Structure of Sym2 D9V+D55V+D130V+D176V Deposited 2012-07-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 123–219（97 aa） Chain D 99–219（121 aa） Chain D 99–122（24 aa）	Mutation：A3R, D9V, Y22H, D55V, D130V, Y143H, D176V Mutation：A3R, D9V, Y22H, D55V, D130V, Y143H, D176V Mutation：A3R, D9V, Y22H, D55V, D130V, Y143H, D176V	PI HYDROGENPHOSPHATE ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.08 Å R-free 0.233
4J9J Structure of designed HisF Deposited 2013-02-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 97–216（120 aa） Fragment：SEE REMARK 999 Chain A 96–220（125 aa） Fragment：SEE REMARK 999	Mutation：S6I,V45A,T76A,D81G,D156G,D202V Mutation：S6I,V45A,T76A,D81G,D156G,D202V	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å R-free 0.297
5TQL Crystal structure of TIM-Barrel protein HisF-C9S Deposited 2016-10-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–253（252 aa）	Mutation：C9S	PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.1 M Tris, pH 7.5, 25% PEG 3350	Resolution 1.90 Å R-free 0.220
5TQL Crystal structure of TIM-Barrel protein HisF-C9S Deposited 2016-10-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–253（252 aa）	Mutation：C9S	PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.1 M Tris, pH 7.5, 25% PEG 3350	Resolution 1.90 Å R-free 0.220
6RTZ Light-Regulation of Imidazole Glycerol Phosphate Synthase by Interference with its Allosteric Machinery through Photo-Sensitive Unnatural Amino Acids Deposited 2019-05-27	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–253（253 aa）	Not recorded	PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；PEG	Resolution 2.87 Å R-free 0.336
6RU0 Light-Regulation of Imidazole Glycerol Phosphate Synthase by Interference with its Allosteric Machinery through Photo-Sensitive Unnatural Amino Acids Deposited 2019-05-27	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–253（253 aa）	Not recorded	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；PEG	Resolution 2.65 Å R-free 0.272
6RU0 Light-Regulation of Imidazole Glycerol Phosphate Synthase by Interference with its Allosteric Machinery through Photo-Sensitive Unnatural Amino Acids Deposited 2019-05-27	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–253（253 aa）	Not recorded	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；PEG	Resolution 2.65 Å R-free 0.272
6RU0 Light-Regulation of Imidazole Glycerol Phosphate Synthase by Interference with its Allosteric Machinery through Photo-Sensitive Unnatural Amino Acids Deposited 2019-05-27	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 1–253（253 aa）	Not recorded	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；PEG	Resolution 2.65 Å R-free 0.272
6VDG Crystal Structure of the Y182A HisF Mutant from Thermotoga maritima Deposited 2019-12-27	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–253（253 aa）	Mutation：Y182A	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；291.15 K；23% PEG 3350, 20mM Potassium Phosphate	Resolution 2.79 Å R-free 0.263
6YMU Imidazole Glycerol Phosphate Synthase Deposited 2020-04-09	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–253（253 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；PEG	Resolution 2.11 Å R-free 0.250
6YMU Imidazole Glycerol Phosphate Synthase Deposited 2020-04-09	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 1–253（253 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；PEG	Resolution 2.11 Å R-free 0.250
6YMU Imidazole Glycerol Phosphate Synthase Deposited 2020-04-09	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain E 1–253（253 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；PEG	Resolution 2.11 Å R-free 0.250
7AC8 Molecular basis for the unique allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex. Deposited 2020-09-10	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–253（253 aa）	Not recorded	GUO [(2R,3S,4R,5R)-5-[4-aminocarbonyl-5-[(E)-[[(2R,3R,4S,5R)-3,4-bis(oxidanyl)-5-(phosphonooxymethyl)oxolan-2-yl]amino]methylideneamino]imidazol-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl dihydrogen phosphate × 1 GLN GLUTAMINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291.15 K；Pentaerythritol (5/4 PO/OH), sodium thiocyanate, HEPES, L-glutamine, ProFAR	Resolution 2.06 Å R-free 0.186
7AC8 Molecular basis for the unique allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex. Deposited 2020-09-10	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–253（253 aa）	Not recorded	GLN GLUTAMINE × 1 PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291.15 K；Pentaerythritol (5/4 PO/OH), sodium thiocyanate, HEPES, L-glutamine, ProFAR	Resolution 2.06 Å R-free 0.186
7AC8 Molecular basis for the unique allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex. Deposited 2020-09-10	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 1–253（253 aa）	Not recorded	GUO [(2R,3S,4R,5R)-5-[4-aminocarbonyl-5-[(E)-[[(2R,3R,4S,5R)-3,4-bis(oxidanyl)-5-(phosphonooxymethyl)oxolan-2-yl]amino]methylideneamino]imidazol-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl dihydrogen phosphate × 1 GLN GLUTAMINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291.15 K；Pentaerythritol (5/4 PO/OH), sodium thiocyanate, HEPES, L-glutamine, ProFAR	Resolution 2.06 Å R-free 0.186
7QC3 HisF from T. maritima Deposited 2021-11-22	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–253（252 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.3；292 K；100 mM TRIS, 23% PEG 3350	Resolution 1.65 Å R-free 0.157
7QC6 HisF_C9A_L50H_I52H mutant (apo) from T. maritima Deposited 2021-11-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–253（252 aa）	Mutation：C9A, L50H, I52H	DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.3；292 K；100 mM TRIS, 23% PEG 3350	Resolution 2.10 Å R-free 0.216
7QC7 HisF-C9A-D11E-V33A_L50H_I52H mutant (apo) from T. maritima Deposited 2021-11-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–253（252 aa）	Mutation：C9A, D11E, V33A, L50H, I52H	MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.3；292 K；100 mM TRIS, 23% PEG 3350	Resolution 1.60 Å R-free 0.159
7QC8 HisF-C9A-D11E-V33A_L50H_I52H mutant in complex with Zn(II) from T. maritima Deposited 2021-11-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–253（252 aa）	Mutation：C9A, D11E, V33A, L50H, I52H	ZN ZINC ION × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.3；292 K；100 mM TRIS, 23% PEG 3350	Resolution 1.80 Å R-free 0.159
7QC9 HisF-C9A-D11E-V33A_L50H_I52H mutant in complex with Ni(II) from T. maritima Deposited 2021-11-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–253（252 aa）	Mutation：C9A, D11E, L50H, I52H	NI NICKEL (II) ION × 1 SO4 SULFATE ION × 1 EDO 1,2-ETHANEDIOL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.3；292 K；100 mM TRIS, 23% PEG 3350	Resolution 1.80 Å R-free 0.189
8S8R An induced-fit motion of a mobile loop Deposited 2024-03-07	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 1–253（253 aa）	Not recorded	PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；277 K；ammonium phosphate	Resolution 1.20 Å R-free 0.208
8S8S An induced-fit motion of a mobile loop Deposited 2024-03-07	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–251（250 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；277 K；ammonium phosphate	Resolution 1.31 Å R-free 0.209

24 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	HIS6_THEMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–253； UniProt 1–253 Author chain C； PDBConstruct 1–253； UniProt 1–253 Author chain E； PDBConstruct 1–253； UniProt 1–253

IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH

THERMOTOGA MARITIMA

UniProt Q9X0C8

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 1–201	Not recorded	IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF × 1 （Q9X0C6） GOL GLYCEROL × 3 GLN GLUTAMINE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.41 Å R-free 0.258
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 1–201	Not recorded	IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF × 1 （Q9X0C6） GOL GLYCEROL × 2 GLN GLUTAMINE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.41 Å R-free 0.258
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain F； UniProt 1–201	Not recorded	IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF × 1 （Q9X0C6） GOL GLYCEROL × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.41 Å R-free 0.258

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 3ZR4	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1GPW Structural evidence for ammonia tunneling across the (beta/alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex. Deposited 2001-11-12	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–201（201 aa）	Not recorded	PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；PROTEIN SOLUTION: 10 MM TRIS (PH 8.0), 1 MM DTT, 1 MM EDTA, 28.8 MG/ML PROTEIN COMPLEX. PRECIPITATE SOLUTION: 15 %[W/V] PEG-8000, 0.9 M AMMONIUM NITRATE, 0.1 M HEPES/HCL (PH 8.5), 10 MM DTT, 5% [V/V] MPD	Resolution 2.40 Å R-free 0.290
1GPW Structural evidence for ammonia tunneling across the (beta/alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex. Deposited 2001-11-12	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–201（201 aa）	Not recorded	PO4 PHOSPHATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；PROTEIN SOLUTION: 10 MM TRIS (PH 8.0), 1 MM DTT, 1 MM EDTA, 28.8 MG/ML PROTEIN COMPLEX. PRECIPITATE SOLUTION: 15 %[W/V] PEG-8000, 0.9 M AMMONIUM NITRATE, 0.1 M HEPES/HCL (PH 8.5), 10 MM DTT, 5% [V/V] MPD	Resolution 2.40 Å R-free 0.290
1GPW Structural evidence for ammonia tunneling across the (beta/alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex. Deposited 2001-11-12	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 1–201（201 aa）	Not recorded	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；PROTEIN SOLUTION: 10 MM TRIS (PH 8.0), 1 MM DTT, 1 MM EDTA, 28.8 MG/ML PROTEIN COMPLEX. PRECIPITATE SOLUTION: 15 %[W/V] PEG-8000, 0.9 M AMMONIUM NITRATE, 0.1 M HEPES/HCL (PH 8.5), 10 MM DTT, 5% [V/V] MPD	Resolution 2.40 Å R-free 0.290
1K9V Structural evidence for ammonia tunelling across the (beta-alpha)8-barrel of the imidazole glycerol phosphate synthase bienzyme complex Deposited 2001-10-31	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain F 1–201（201 aa）	Not recorded	ACY ACETIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；298 K；PEG 200, sodium acetate, DTT, calcium chloride, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 2.40 Å R-free 0.278
1KXJ The Crystal Structure of Glutamine Amidotransferase from Thermotoga maritima Deposited 2002-01-31	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–201（201 aa）	Not recorded	PO4 PHOSPHATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；298 K；2 M mono-Ammonium dihydrogen Phosphate, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K	Resolution 2.80 Å R-free 0.274
1KXJ The Crystal Structure of Glutamine Amidotransferase from Thermotoga maritima Deposited 2002-01-31	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–201（201 aa）	Not recorded	PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；298 K；2 M mono-Ammonium dihydrogen Phosphate, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K	Resolution 2.80 Å R-free 0.274
2WJZ Crystal structure of (HisH) K181A Y138A mutant of imidazoleglycerolphosphate synthase (HisH HisF) which displays constitutive glutaminase activity Deposited 2009-06-02	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–201（201 aa）	Mutation：YES	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；PEG8K 10-12%, 100 MM HEPES PH = 8.5 22.5MM NH4NO3 / NH4AC 5% (V/V) MPD 10 MM DTT 20 MM L-GLN PROT. CONC.= 12 MG/ML	Resolution 2.60 Å R-free 0.218
2WJZ Crystal structure of (HisH) K181A Y138A mutant of imidazoleglycerolphosphate synthase (HisH HisF) which displays constitutive glutaminase activity Deposited 2009-06-02	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 1–201（201 aa）	Mutation：YES	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；PEG8K 10-12%, 100 MM HEPES PH = 8.5 22.5MM NH4NO3 / NH4AC 5% (V/V) MPD 10 MM DTT 20 MM L-GLN PROT. CONC.= 12 MG/ML	Resolution 2.60 Å R-free 0.218
2WJZ Crystal structure of (HisH) K181A Y138A mutant of imidazoleglycerolphosphate synthase (HisH HisF) which displays constitutive glutaminase activity Deposited 2009-06-02	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–201（201 aa）	Mutation：YES	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；PEG8K 10-12%, 100 MM HEPES PH = 8.5 22.5MM NH4NO3 / NH4AC 5% (V/V) MPD 10 MM DTT 20 MM L-GLN PROT. CONC.= 12 MG/ML	Resolution 2.60 Å R-free 0.218
6RTZ Light-Regulation of Imidazole Glycerol Phosphate Synthase by Interference with its Allosteric Machinery through Photo-Sensitive Unnatural Amino Acids Deposited 2019-05-27	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–201（201 aa）	Not recorded	PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；PEG	Resolution 2.87 Å R-free 0.336
6RU0 Light-Regulation of Imidazole Glycerol Phosphate Synthase by Interference with its Allosteric Machinery through Photo-Sensitive Unnatural Amino Acids Deposited 2019-05-27	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–201（201 aa）	Not recorded	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；PEG	Resolution 2.65 Å R-free 0.272
6RU0 Light-Regulation of Imidazole Glycerol Phosphate Synthase by Interference with its Allosteric Machinery through Photo-Sensitive Unnatural Amino Acids Deposited 2019-05-27	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–201（201 aa）	Not recorded	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；PEG	Resolution 2.65 Å R-free 0.272
6RU0 Light-Regulation of Imidazole Glycerol Phosphate Synthase by Interference with its Allosteric Machinery through Photo-Sensitive Unnatural Amino Acids Deposited 2019-05-27	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 1–201（201 aa）	Not recorded	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；PEG	Resolution 2.65 Å R-free 0.272
6YMU Imidazole Glycerol Phosphate Synthase Deposited 2020-04-09	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–201（201 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；PEG	Resolution 2.11 Å R-free 0.250
6YMU Imidazole Glycerol Phosphate Synthase Deposited 2020-04-09	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 1–201（201 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；PEG	Resolution 2.11 Å R-free 0.250
6YMU Imidazole Glycerol Phosphate Synthase Deposited 2020-04-09	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain F 1–201（201 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；PEG	Resolution 2.11 Å R-free 0.250
7AC8 Molecular basis for the unique allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex. Deposited 2020-09-10	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–201（201 aa）	Mutation：C84A	GUO [(2R,3S,4R,5R)-5-[4-aminocarbonyl-5-[(E)-[[(2R,3R,4S,5R)-3,4-bis(oxidanyl)-5-(phosphonooxymethyl)oxolan-2-yl]amino]methylideneamino]imidazol-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl dihydrogen phosphate × 1 GLN GLUTAMINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291.15 K；Pentaerythritol (5/4 PO/OH), sodium thiocyanate, HEPES, L-glutamine, ProFAR	Resolution 2.06 Å R-free 0.186
7AC8 Molecular basis for the unique allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex. Deposited 2020-09-10	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–201（201 aa）	Mutation：C84A	GLN GLUTAMINE × 1 PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291.15 K；Pentaerythritol (5/4 PO/OH), sodium thiocyanate, HEPES, L-glutamine, ProFAR	Resolution 2.06 Å R-free 0.186
7AC8 Molecular basis for the unique allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex. Deposited 2020-09-10	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 1–201（201 aa）	Mutation：C84A	GUO [(2R,3S,4R,5R)-5-[4-aminocarbonyl-5-[(E)-[[(2R,3R,4S,5R)-3,4-bis(oxidanyl)-5-(phosphonooxymethyl)oxolan-2-yl]amino]methylideneamino]imidazol-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl dihydrogen phosphate × 1 GLN GLUTAMINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291.15 K；Pentaerythritol (5/4 PO/OH), sodium thiocyanate, HEPES, L-glutamine, ProFAR	Resolution 2.06 Å R-free 0.186

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

View Construct and Data Evidence

UniProt name	HIS5_THEMA
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–201； UniProt 1–201 Author chain D； PDBConstruct 1–200； UniProt 1–201 Author chain F； PDBConstruct 1–200； UniProt 1–201

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.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3zr4
Deposition date deposition_date	2011-06-13
Structure title title	STRUCTURAL EVIDENCE FOR AMMONIA TUNNELING ACROSS THE (BETA-ALPHA)8 BARREL OF THE IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE BIENZYME COMPLEX
Keywords keywords	TRANSFERASE; TRANSFERASE
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	36.38 Å
Radius of gyration Rg (electron density) rg_electron	35.67 Å
Forward intensity I(0) i0	327559000.00
Molecular weight molecular_weight	149490.0 kDa
Excluded volume excluded_volume	188610 Å³
Envelope volume envelope_volume	239160 Å³
Hydration-shell volume shell_volume	55125 Å³
Envelope diameter envelope_diameter	121.2 Å
Shell Rg shell_rg	42.67 Å
Envelope Rg envelope_rg	35.31 Å
Shape Rg shape_rg	35.66 Å
Total Rg total_rg	36.16 Å
Total atoms total_atoms	10524
Residues n_residues	1333
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	114.0 Å
Rg (real space) rg_real	36.24 Å
Rg uncertainty (real space) rg_real_error	0.69 Å
I(0) (real space) i0_real	3.2760e+08
I(0) uncertainty (real space) i0_real_error	5.3190e+06
Rg (reciprocal space) rg_reciprocal	36.33 Å
I(0) (reciprocal space) i0_reciprocal	327600000.0000
Solution quality estimate total_estimate	0.9001
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	47.7 Å
Skewness Skewness skewness	0.170
Kurtosis Kurtosis kurtosis	-0.545
Angular range angular_range	— – 0.2150 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	130600000.0000
Real-space data points n_real_points	44
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.943; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.869

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF
Molecular weight formula_weight	27753.9 kDa
EC 编号 ec_number	4.1.3.-
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,E
Atom count atom_count	10728

MLAKRIIACLDVKDGRVVKGTNFENLRDSGDPVELGKFYSEIGIDELVFLDITASVEKRKTMLELVEKVAEQIDIPFTVGGGIHDFETASELILRGADKVSINTAAVENPSLITQIAQTFGSQAVVVAIDAKRVDGEFMVFTYSGKKNTGILLRDWVVEVEKRGAGEILLTSIDRDGTKSGYDTEMIRFVRPLTTLPIIASGGAGKMEHFLEAFLAGADAALAASVFHFREIDVRELKEYLKKHGVNVRLEGL

来源 Source

来源生物 organism	THERMOTOGA MARITIMA
NCBI Class编号 ncbi_taxonomy_id	2336
宿主生物 host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH
Molecular weight formula_weight	23130.6 kDa
EC 编号 ec_number	2.4.2.-
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D,F

MRIGIISVGPGNIMNLYRGVKRASENFEDVSIELVESPRNDLYDLLFIPGVGHFGEGMRRLRENDLIDFVRKHVEDERYVVGVCLGMQLLFEESEEAPGVKGLSLIEGNVVKLRSRRLPHMGWNEVIFKDTFPNGYYYFVHTYRAVCEEEHVLGTTEYDGEIFPSAVRKGRILGFQFHPEKSSKIGRKLLEKVIECSLSRR

来源 Source

来源生物 organism	THERMOTOGA MARITIMA
NCBI Class编号 ncbi_taxonomy_id	2336
宿主生物 host_organism	ESCHERICHIA COLI

Entity 3 Entity 3 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	7

Entity 4 Entity 4 non-polymer

Description description	GLUTAMINE
Molecular weight formula_weight	146.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	204

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7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d3zr4a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.2 — Ribulose-phoshate binding barrel
Family Family family	c.1.2.1 — Histidine biosynthesis enzymes

Domain ID domain_id	d3zr4b_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.23 — Flavodoxin-like
Superfamily Superfamily superfamily	c.23.16 — Class I glutamine amidotransferase-like
Family Family family	c.23.16.1 — Class I glutamine amidotransferases (GAT)

Domain ID domain_id	d3zr4c_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.2 — Ribulose-phoshate binding barrel
Family Family family	c.1.2.1 — Histidine biosynthesis enzymes

Domain ID domain_id	d3zr4d_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.23 — Flavodoxin-like
Superfamily Superfamily superfamily	c.23.16 — Class I glutamine amidotransferase-like
Family Family family	c.23.16.1 — Class I glutamine amidotransferases (GAT)

Domain ID domain_id	d3zr4e_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.2 — Ribulose-phoshate binding barrel
Family Family family	c.1.2.1 — Histidine biosynthesis enzymes

Domain ID domain_id	d3zr4f_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.23 — Flavodoxin-like
Superfamily Superfamily superfamily	c.23.16 — Class I glutamine amidotransferase-like
Family Family family	c.23.16.1 — Class I glutamine amidotransferases (GAT)

CATH v4.4 (6 domains)

Domain ID domain_id	3zr4A00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	70 — Aldolase class I

Domain ID domain_id	3zr4B00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	880 — Class I glutamine amidotransferase (GATase) domain

Domain ID domain_id	3zr4C00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	70 — Aldolase class I

Domain ID domain_id	3zr4D00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	880 — Class I glutamine amidotransferase (GATase) domain

Domain ID domain_id	3zr4E00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	70 — Aldolase class I

Domain ID domain_id	3zr4F00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	880 — Class I glutamine amidotransferase (GATase) domain

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8. Citations (2)

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Unit-cell length a length_a	85.399 Å
Unit-cell length b length_b	85.399 Å
Unit-cell length c length_c	171.109 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	9

Space group space_group	P 32
Space-group number int_tables_number	145
Crystal system crystal_system	—

Resolution resolution	2.410 Å
Low-resolution limit resolution_low	55.960 Å
R factor r_factor	0.1990
R_work r_work	0.1936
R_free r_free	0.2577

fit	/app/data/saxs_computation/zr/3zr4/3zr4.fit
pddf	/app/data/pr_computation/zr/3zr4/3zr4.pr.out
profile	/app/data/saxs_computation/zr/3zr4/3zr4.dat

STRUCTURAL EVIDENCE FOR AMMONIA TUNNELING ACROSS THE (BETA-ALPHA)8 BARREL OF THE IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE BIENZYME COMPLEX

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

IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF

State in the Current Structure

Other States of the Same Protein in the Database

IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH

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

6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)