SAXSdb — 1cm3

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

HISTIDINE-CONTAINING PROTEIN

Escherichia coli

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 1–85	Mutation：HIS15ASP	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 5.4；pH 5.4	Resolution 1.60 Å

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 1CM3	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CM2 STRUCTURE OF HIS15ASP HPR AFTER HYDROLYSIS OF RINGED SPECIES. Deposited 1999-05-13	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–85（85 aa）	Mutation：HIS15ASP	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；pH 4.6	Resolution 1.80 Å
1GGR COMPLEX OF ENZYME IIAGLC AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE Deposited 2000-09-18	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–85（85 aa）	Not recorded	PO3 PHOSPHITE ION × 1	SOLUTION NMR NMR measurement conditions pH 7.1；308 K；Ionic strength (raw mmCIF value) 10 mM SODIUM PHOSPHATE	Resolution not provided
1HDN THE HIGH-RESOLUTION STRUCTURE OF THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI DETERMINED BY RESTRAINED MOLECULAR DYNAMICS FROM NMR NUCLEAR OVERHAUSER EFFECT DATA Deposited 1994-02-10	Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–85（85 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1J6T COMPLEX OF ENZYME IIAMTL AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE Deposited 2002-08-14	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–85（85 aa）	Not recorded	PO3 PHOSPHITE ION × 1	SOLUTION NMR NMR measurement conditions pH 7；308 K；Ionic strength (raw mmCIF value) 10 mM SODIUM PHOSPHATE	Resolution not provided
1OPD HISTIDINE-CONTAINING PROTEIN (HPR), MUTANT WITH SER 46 REPLACED BY ASP (S46D) Deposited 1996-08-01	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–85（85 aa）	Mutation：S46D	SO4 SULFATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.50 Å R-free 0.234
1PFH THE PHOSPHORYLATED FORM OF THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR Deposited 1995-08-18	Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–85（85 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1POH THE 2.0 ANGSTROMS RESOLUTION STRUCTURE OF ESCHERICHIA COLI HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR: A REDETERMINATION Deposited 1993-10-19	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–85（85 aa）	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å
1VRC Complex of enzyme IIAmannose and the histidine-containing phosphocarrier protein HPr from escherichia coli nmr, restrained regularized mean structure Deposited 2005-02-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–85（85 aa） Chain D 1–85（85 aa）	Not recorded	PO3 PHOSPHITE ION × 2	SOLUTION NMR NMR measurement conditions pH 6.5；308 K；Ionic strength (raw mmCIF value) 40 mM SODIUM PHOSPHATE	Resolution not provided
2JEL JEL42 FAB/HPR COMPLEX Deposited 1998-02-24	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain P 1–85（85 aa）	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.8；pH 5.8	Resolution 2.50 Å R-free 0.280
2LRK Solution Structures of the IIA(Chitobiose)-HPr complex of the N,N'-Diacetylchitobiose Deposited 2012-04-06	Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 1–85（85 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.4；308 K；Ionic strength (raw mmCIF value) 0.02；Pressure ambient NMR sample composition 1.0 mM [U-100% 15N] HPr/IIAChb complex, 1.0 mM [U-100% 13C; U-100% 15N] HPR/IIAChb complex, 1.0 mM [U-100% 13C; U-100% 15N] HPR/IIAChb complex, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1.0 mM [U-100% 15N] HPr/IIAChb complex, 1.0 mM [U-100% 13C; U-100% 15N] HPR/IIAChb complex, 1.0 mM [U-100% 13C; U-100% 15N] HPR/IIAChb complex, 100% D2O \| 100% D2O	Resolution not provided
2LRL Solution Structures of the IIA(Chitobiose)-HPr complex of the N,N'-Diacetylchitobiose Branch of the Escherichia coli Phosphotransferase System Deposited 2012-04-06	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 1–85（85 aa）	Not recorded	PO3 PHOSPHITE ION × 1	SOLUTION NMR NMR measurement conditions pH 7.4；308 K；Ionic strength (raw mmCIF value) 0.02；Pressure ambient NMR sample composition 1.0 mM [U-99% 13C; U-99% 15N] protein, 1.0 mM D2O, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
3CCD 1.0 A Structure of Post-Succinimide His15Asp HPr Deposited 2008-02-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–85（85 aa） Chain B 1–85（85 aa）	Mutation：His15Asp Mutation：His15Asp	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.4；287 K；0.1M citrate phosphate buffer, 25% saturated ammonium sulphate, pH 4.4, VAPOR DIFFUSION, HANGING DROP, temperature 287K	Resolution 1.00 Å R-free 0.205
3CCD 1.0 A Structure of Post-Succinimide His15Asp HPr Deposited 2008-02-25	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–85（85 aa）	Mutation：His15Asp	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.4；287 K；0.1M citrate phosphate buffer, 25% saturated ammonium sulphate, pH 4.4, VAPOR DIFFUSION, HANGING DROP, temperature 287K	Resolution 1.00 Å R-free 0.205
3CCD 1.0 A Structure of Post-Succinimide His15Asp HPr Deposited 2008-02-25	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–85（85 aa）	Mutation：His15Asp	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.4；287 K；0.1M citrate phosphate buffer, 25% saturated ammonium sulphate, pH 4.4, VAPOR DIFFUSION, HANGING DROP, temperature 287K	Resolution 1.00 Å R-free 0.205
3EZA COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE Deposited 1998-11-03	Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–85（85 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；313 K	Resolution not provided
3EZB COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI Deposited 1998-11-03	Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–85（85 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；313 K	Resolution not provided
3EZE COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE Deposited 1998-11-04	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–85（85 aa）	Not recorded	PO3 PHOSPHITE ION × 1	SOLUTION NMR NMR measurement conditions pH 7；313 K	Resolution not provided
4XWJ Histidine-containing phosphocarrier protein (HPr) and antisigma factor Rsd complex Deposited 2015-01-29	Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–85（85 aa）	Mutation：F2S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；287.15 K；0.1 M NaCl, 0.1 M HEPES (pH 7.5), 1.6 M ammonium sulfate	Resolution 2.10 Å R-free 0.299
5YA0 Crystal structure of LsrK and HPr complex Deposited 2017-08-29	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–85（85 aa）	Not recorded	HEZ HEXANE-1,6-DIOL × 1 PO4 PHOSPHATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；293 K；5~20% (v/v) PEG-400, 0.1 M sodium phosphate-citrate (pH 4.2), and 0.2 M lithium sulfate	Resolution 3.00 Å R-free 0.239
5YA0 Crystal structure of LsrK and HPr complex Deposited 2017-08-29	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–85（85 aa）	Not recorded	HEZ HEXANE-1,6-DIOL × 1 PO4 PHOSPHATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；293 K；5~20% (v/v) PEG-400, 0.1 M sodium phosphate-citrate (pH 4.2), and 0.2 M lithium sulfate	Resolution 3.00 Å R-free 0.239
5YA1 crystal structure of LsrK-HPr complex with ATP Deposited 2017-08-29	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–85（85 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1 HEZ HEXANE-1,6-DIOL × 2 PO4 PHOSPHATE ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；5~20% (v/v) PEG-400, 0.1M sodium phosphate-citrate (pH 4.2), 0.2M lithium sulfate	Resolution 2.70 Å R-free 0.254
5YA1 crystal structure of LsrK-HPr complex with ATP Deposited 2017-08-29	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–85（85 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1 HEZ HEXANE-1,6-DIOL × 2 PO4 PHOSPHATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；5~20% (v/v) PEG-400, 0.1M sodium phosphate-citrate (pH 4.2), 0.2M lithium sulfate	Resolution 2.70 Å R-free 0.254
5YA2 Crystal structure of LsrK-HPr complex with ADP Deposited 2017-08-30	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–85（85 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1 HEZ HEXANE-1,6-DIOL × 1 PO4 PHOSPHATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；5~20%(v/v) PEG-400, 0.1M sodium phosphate-citrate (pH 4.2), 0.2M lithium sulfate	Resolution 2.70 Å R-free 0.255
5YA2 Crystal structure of LsrK-HPr complex with ADP Deposited 2017-08-30	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–85（85 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1 HEZ HEXANE-1,6-DIOL × 1 PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；5~20%(v/v) PEG-400, 0.1M sodium phosphate-citrate (pH 4.2), 0.2M lithium sulfate	Resolution 2.70 Å R-free 0.255
6KCR X-ray structure of the MtlR-HPr complex from Escherichia coli Deposited 2019-06-28	Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–85（85 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；289 K；100 mM Tris-HCl (pH 8.5), 200 mM Mg-acetate, 15% polyethylene glycol (PEG) 8000	Resolution 3.50 Å R-free 0.260
6KCR X-ray structure of the MtlR-HPr complex from Escherichia coli Deposited 2019-06-28	Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–85（85 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；289 K；100 mM Tris-HCl (pH 8.5), 200 mM Mg-acetate, 15% polyethylene glycol (PEG) 8000	Resolution 3.50 Å R-free 0.260
9S8B Structure of glycogen phosphorylase - dimeric form - in complex with HPr from Escherichia coli Deposited 2025-08-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–85（85 aa） Chain D 1–85（85 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.79 Å
9S8K Structure of glycogen phosphorylase - tetrameric form - in complex with HPr from Escherichia coli Deposited 2025-08-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–85（85 aa） Chain F 1–85（85 aa） Chain G 1–85（85 aa） Chain H 1–85（85 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.06 Å

22 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PTHP_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–85； UniProt 1–85

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	1cm3
Deposition date deposition_date	1999-05-13
Structure title title	HIS15ASP HPR FROM E. COLI
Keywords keywords	PHOSPHOTRANSFERASE, 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	13.23 Å
Radius of gyration Rg (electron density) rg_electron	11.66 Å
Forward intensity I(0) i0	1808110.00
Molecular weight molecular_weight	9081.0 kDa
Excluded volume excluded_volume	11401 Å³
Envelope volume envelope_volume	12476 Å³
Hydration-shell volume shell_volume	9278 Å³
Envelope diameter envelope_diameter	39.7 Å
Shell Rg shell_rg	17.18 Å
Envelope Rg envelope_rg	11.92 Å
Shape Rg shape_rg	11.65 Å
Total Rg total_rg	13.08 Å
Total atoms total_atoms	782
Residues n_residues	85
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	46.5 Å
Rg (real space) rg_real	13.14 Å
Rg uncertainty (real space) rg_real_error	0.30 Å
I(0) (real space) i0_real	1.8080e+06
I(0) uncertainty (real space) i0_real_error	1.7830e+04
Rg (reciprocal space) rg_reciprocal	13.14 Å
I(0) (reciprocal space) i0_reciprocal	1808000.0000
Solution quality estimate total_estimate	0.7727
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	17.1 Å
Skewness Skewness skewness	0.115
Kurtosis Kurtosis kurtosis	-0.339
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	353000.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.682; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1cm3a_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.94 — HPr-like
Superfamily Superfamily superfamily	d.94.1 — HPr-like
Family Family family	d.94.1.1 — HPr-like

CATH v4.4 (1 domains)

Domain ID domain_id	1cm3A00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1340 — Histidine-containing Protein; Chain: A;
Homologous superfamily homologous superfamily	10 — HPr-like

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8. Citations (1)

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Unit-cell length a length_a	25.570 Å
Unit-cell length b length_b	45.340 Å
Unit-cell length c length_c	27.620 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	104.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	2

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.600 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	0.1910
R_work r_work	0.1910
R_free r_free	—

Description description	HISTIDINE-CONTAINING PROTEIN
Molecular weight formula_weight	9106.3 kDa
Mutation mutation	HIS15ASP
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1025

HIS15ASP HPR FROM E. COLI

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

HISTIDINE-CONTAINING PROTEIN

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	81

fit	/app/data/saxs_computation/cm/1cm3/1cm3.fit
pddf	/app/data/pr_computation/cm/1cm3/1cm3.pr.out
profile	/app/data/saxs_computation/cm/1cm3/1cm3.dat