SAXSdb — 1dhp

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

DIHYDRODIPICOLINATE SYNTHASE

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 1–292 Chain B； UniProt 1–292	Mutation：A207T	K POTASSIUM ION × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.30 Å
2	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–292 Chain B； UniProt 1–292	Mutation：A207T	K POTASSIUM ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.30 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 1DHP	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1S5T Crystal Structure Analysis of a mutant of DIHYDRODIPICOLINATE SYNTHASE--residue thr44 to val44 Deposited 2004-01-21	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Chain B 1–292（292 aa）	Mutation：T44V Mutation：T44V	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；277 K；Drop contains: potassium phosphate (0.0012ml, 1.8M, pH10), N-octyl-beta-R-glucopyrandoside (0.0006ml, 6% w/v), VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.30 Å R-free 0.213
1S5V Crystal Structure Analysis of a mutant of DIHYDRODIPICOLINATE SYNTHASE--residue Tyr107 to Phe107 Deposited 2004-01-21	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Chain B 1–292（292 aa）	Mutation：Y107F Mutation：Y107F	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；277 K；potassium phosphate (0.0012ml, 1.8M, pH10), N-octyl-beta-R-glucopyrandoside (0.0006ml, 6% w/v), VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.35 Å R-free 0.232
1S5V Crystal Structure Analysis of a mutant of DIHYDRODIPICOLINATE SYNTHASE--residue Tyr107 to Phe107 Deposited 2004-01-21	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–292（292 aa） Chain B 1–292（292 aa）	Mutation：Y107F Mutation：Y107F	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；277 K；potassium phosphate (0.0012ml, 1.8M, pH10), N-octyl-beta-R-glucopyrandoside (0.0006ml, 6% w/v), VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.35 Å R-free 0.232
1S5V Crystal Structure Analysis of a mutant of DIHYDRODIPICOLINATE SYNTHASE--residue Tyr107 to Phe107 Deposited 2004-01-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–292（292 aa）	Mutation：Y107F	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；277 K；potassium phosphate (0.0012ml, 1.8M, pH10), N-octyl-beta-R-glucopyrandoside (0.0006ml, 6% w/v), VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.35 Å R-free 0.232
1S5V Crystal Structure Analysis of a mutant of DIHYDRODIPICOLINATE SYNTHASE--residue Tyr107 to Phe107 Deposited 2004-01-21	Different construct 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 B 1–292（292 aa）	Mutation：Y107F	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；277 K；potassium phosphate (0.0012ml, 1.8M, pH10), N-octyl-beta-R-glucopyrandoside (0.0006ml, 6% w/v), VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.35 Å R-free 0.232
1S5W Crystal Structure Analysis of a mutant of DIHYDRODIPICOLINATE SYNTHASE--residue Tyr133 to Phe133 Deposited 2004-01-21	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Chain B 1–292（292 aa）	Mutation：Y133F Mutation：Y133F	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；277 K；Drop contains: potassium phosphate (0.0012ml, 1.8M, pH10), N-octyl-beta-R-glucopyrandoside (0.0006ml, 6% w/v), VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.32 Å R-free 0.211
1YXC Structure of E. coli dihydrodipicolinate synthase to 1.9 A Deposited 2005-02-20	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Chain B 1–292（292 aa）	Not recorded	K POTASSIUM ION × 4 CL CHLORIDE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；276 K；1.8M potassium phosphate, pH 10, VAPOR DIFFUSION, HANGING DROP, temperature 276K	Resolution 1.90 Å R-free 0.211
1YXD Structure of E. coli dihydrodipicolinate synthase bound with allosteric inhibitor (S)-lysine to 2.0 A Deposited 2005-02-20	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Chain B 1–292（292 aa）	Not recorded	K POTASSIUM ION × 4 CL CHLORIDE ION × 4 LYS LYSINE × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；276 K；1.8M potassium phosphate, pH 10, VAPOR DIFFUSION, HANGING DROP, temperature 276K	Resolution 2.00 Å R-free 0.186
2A6L Dihydrodipicolinate synthase (E. coli)- mutant R138H Deposited 2005-07-03	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Chain B 1–292（292 aa）	Mutation：R138H Mutation：R138H	K POTASSIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 10；285 K；protein solution (~5 mg/ml in Tris.HCl 20 mM, pH 8, 2.5 uL), precipitant (K2HPO4 1.8 M, pH 10, 1.2 uL), and N-octyl- -R-glucopyranoside (6% w/v, 0.6 uL), VAPOR DIFFUSION, temperature 12K	Resolution 2.05 Å R-free 0.213
2A6N Dihydrodipicolinate synthase (E. coli)- mutant R138A Deposited 2005-07-03	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Chain B 1–292（292 aa）	Mutation：R138A Mutation：R138A	K POTASSIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；284 K；protein solution (~5 mg/ml in Tris.HCl 20 mM, pH 8, 2.5 uL), precipitant (K2HPO4 1.8 M, pH 10, 1.2 uL), and N-octyl- -R-glucopyranoside (6% w/v, 0.6 uL), VAPOR DIFFUSION, HANGING DROP, temperature 284K	Resolution 1.94 Å R-free 0.191
2ATS Dihydrodipicolinate synthase co-crystallised with (S)-lysine Deposited 2005-08-26	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 1–292（292 aa） Chain B 1–292（292 aa）	Not recorded	K POTASSIUM ION × 2 CL CHLORIDE ION × 2 DLY D-LYSINE × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；284 K；20mM Tris HCl, 10mM (S)-lysine, pH 8, 1.8M K2HPO4, pH 10, N-octyl-R-glucopyranoside, VAPOR DIFFUSION, HANGING DROP, temperature 284K	Resolution 1.90 Å R-free 0.202
2OJP The crystal structure of a dimeric mutant of Dihydrodipicolinate synthase from E.coli- DHDPS-L197Y Deposited 2007-01-13	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 1–292（292 aa） Chain B 1–292（292 aa）	Mutation：L197Y Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L197Y Non-standard monomer：Yes (specific site not provided by mmCIF)	GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；277 K；PEG 1500, TRIS HCL, pH 8.00, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.70 Å R-free 0.228
2PUR Structure of dihydrodipicolinate synthase mutant Thr44Ser at 1.7 A. Deposited 2007-05-09	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Chain B 1–292（292 aa）	Mutation：T44S Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：T44S Non-standard monomer：Yes (specific site not provided by mmCIF)	K POTASSIUM ION × 4 PO4 PHOSPHATE ION × 4 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；280 K；Drops contained: protein solution (~5 mg mL-1 in Tris.HCl 20 mM, pH 8, 2.5 uL), precipitant (K2HPO4 1.8 M, pH 10, 1.2 uL), and N-octyl-beta-R-glucopyranoside (6% w/v, 0.6 uL). Crystals appeared after 3-5 days and grew to dimensions of up to 0.2 mm., VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 1.70 Å R-free 0.207
3C0J Structure of E. coli dihydrodipicolinate synthase complexed with hydroxypyruvate Deposited 2008-01-21	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Chain B 1–292（292 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	K POTASSIUM ION × 4 GOL GLYCEROL × 6 PO4 PHOSPHATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；285 K；1.8M K2HPO4 (pH 10.0), 6% w/v N-octyl-D-glucopyranoside, VAPOR DIFFUSION, HANGING DROP, temperature 285K	Resolution 2.40 Å R-free 0.237
3C0J Structure of E. coli dihydrodipicolinate synthase complexed with hydroxypyruvate Deposited 2008-01-21	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–292（292 aa） Chain B 1–292（292 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	K POTASSIUM ION × 2 GOL GLYCEROL × 3 PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；285 K；1.8M K2HPO4 (pH 10.0), 6% w/v N-octyl-D-glucopyranoside, VAPOR DIFFUSION, HANGING DROP, temperature 285K	Resolution 2.40 Å R-free 0.237
3DEN Structure of E. coli DHDPS mutant Y107W Deposited 2008-06-10	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Chain B 1–292（292 aa）	Mutation：Y107W Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y107W Non-standard monomer：Yes (specific site not provided by mmCIF)	K POTASSIUM ION × 4 GOL GLYCEROL × 6 PO4 PHOSPHATE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；284 K；1.8M K2HPO4, 6% (w/v) N-octyl-beta-R-glucopyranoside , pH 10, VAPOR DIFFUSION, HANGING DROP, temperature 284K	Resolution 2.20 Å R-free 0.241
3DU0 E. coli dihydrodipicolinate synthase with first substrate, pyruvate, bound in active site Deposited 2008-07-16	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Chain B 1–292（292 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	K POTASSIUM ION × 8 GOL GLYCEROL × 6 CL CHLORIDE ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions hanging drop；pH 10；277 K；1.8M K2HPO4, N-octyl-beta-(R)-glucopyranoside, pH 10, hanging drop, temperature 277K	Resolution 2.00 Å R-free 0.245
3I7Q Dihydrodipicolinate synthase mutant - K161A Deposited 2009-07-08	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 1–292（292 aa） Fragment：dihydrodipicolinate synthase Chain B 1–292（292 aa） Fragment：dihydrodipicolinate synthase	Mutation：K161A Mutation：K161A	GOL GLYCEROL × 5 K POTASSIUM ION × 4 PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；276 K；1.8M POTASSIUM PHOSPHATE, PH 10, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 276K	Resolution 2.00 Å R-free 0.237
3I7Q Dihydrodipicolinate synthase mutant - K161A Deposited 2009-07-08	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Fragment：dihydrodipicolinate synthase Chain B 1–292（292 aa） Fragment：dihydrodipicolinate synthase	Mutation：K161A Mutation：K161A	GOL GLYCEROL × 10 K POTASSIUM ION × 8 PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；276 K；1.8M POTASSIUM PHOSPHATE, PH 10, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 276K	Resolution 2.00 Å R-free 0.237
3I7R Dihydrodipicolinate synthase - K161R Deposited 2009-07-08	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 1–292（292 aa） Fragment：dihydrodipicolinate synthase Chain B 1–292（292 aa） Fragment：dihydrodipicolinate synthase	Mutation：K161R Mutation：K161R	K POTASSIUM ION × 4 GOL GLYCEROL × 6 CL CHLORIDE ION × 2 PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；276 K；1.8M POTASSIUM PHOSPHATE, PH 10, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 276K	Resolution 2.10 Å R-free 0.230
3I7R Dihydrodipicolinate synthase - K161R Deposited 2009-07-08	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Fragment：dihydrodipicolinate synthase Chain B 1–292（292 aa） Fragment：dihydrodipicolinate synthase	Mutation：K161R Mutation：K161R	K POTASSIUM ION × 8 GOL GLYCEROL × 12 CL CHLORIDE ION × 4 PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；276 K；1.8M POTASSIUM PHOSPHATE, PH 10, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 276K	Resolution 2.10 Å R-free 0.230
3I7S Dihydrodipicolinate synthase mutant - K161A - with the substrate pyruvate bound in the active site. Deposited 2009-07-08	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 1–292（292 aa） Fragment：dihydrodipicolinate synthase Chain B 1–292（292 aa） Fragment：dihydrodipicolinate synthase	Mutation：K161A Mutation：K161A	GOL GLYCEROL × 8 K POTASSIUM ION × 6 PYR PYRUVIC ACID × 2 PO4 PHOSPHATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；276 K；1.8M POTASSIUM PHOSPHATE, PH 10, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 276K	Resolution 2.30 Å R-free 0.236
3I7S Dihydrodipicolinate synthase mutant - K161A - with the substrate pyruvate bound in the active site. Deposited 2009-07-08	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Fragment：dihydrodipicolinate synthase Chain B 1–292（292 aa） Fragment：dihydrodipicolinate synthase	Mutation：K161A Mutation：K161A	GOL GLYCEROL × 16 K POTASSIUM ION × 12 PYR PYRUVIC ACID × 4 PO4 PHOSPHATE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；276 K；1.8M POTASSIUM PHOSPHATE, PH 10, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 276K	Resolution 2.30 Å R-free 0.236
4EOU Crystal structure of E. coli dihydrodipicolinate synthase with pyruvate and succinic semi-aldehyde bound in active site Deposited 2012-04-15	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Chain B 1–292（292 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	K POTASSIUM ION × 8 GOL GLYCEROL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；277 K；6% w/v N-octyl-R-glucopyranoside, 1.8 M potassium phosphate dibasic, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.30 Å R-free 0.198

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

View Construct and Data Evidence

UniProt name	DAPA_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–292； UniProt 1–292 Author chain B； PDBConstruct 1–292； UniProt 1–292

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	1dhp
Deposition date deposition_date	1995-02-09
Structure title title	DIHYDRODIPICOLINATE SYNTHASE
Keywords keywords	SYNTHASE, DIHYDRODIPICOLINATE; SYNTHASE
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	31.81 Å
Radius of gyration Rg (electron density) rg_electron	31.04 Å
Forward intensity I(0) i0	62730400.00
Molecular weight molecular_weight	62608.0 kDa
Excluded volume excluded_volume	78430 Å³
Envelope volume envelope_volume	102210 Å³
Hydration-shell volume shell_volume	27159 Å³
Envelope diameter envelope_diameter	98.3 Å
Shell Rg shell_rg	38.98 Å
Envelope Rg envelope_rg	29.70 Å
Shape Rg shape_rg	31.02 Å
Total Rg total_rg	31.80 Å
Total atoms total_atoms	4382
Residues n_residues	584
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	97.1 Å
Rg (real space) rg_real	31.84 Å
Rg uncertainty (real space) rg_real_error	0.67 Å
I(0) (real space) i0_real	6.2730e+07
I(0) uncertainty (real space) i0_real_error	1.0320e+06
Rg (reciprocal space) rg_reciprocal	31.83 Å
I(0) (reciprocal space) i0_reciprocal	62730000.0000
Solution quality estimate total_estimate	0.8567
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	27.2 Å
Skewness Skewness skewness	0.153
Kurtosis Kurtosis kurtosis	-0.964
Angular range angular_range	— – 0.2500 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	10280000.0000
Real-space data points n_real_points	51
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.793; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.899; Smooth: 0.857

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	DIHYDRODIPICOLINATE SYNTHASE
Molecular weight formula_weight	31304.9 kDa
EC 编号 ec_number	4.2.1.52
Mutation mutation	A207T
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	4726

MFTGSIVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGANATAEAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGIKEATGNLTRVNQIKELVSDDFVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMCKLAAEGHFAEARVINQRLMPLHNKLFVEPNPIPVKWACKELGLVATDTLRLPMTPITDSGRETVRAALKHAGLL

来源 Source

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

Entity 2 Entity 2 non-polymer

Description description	POTASSIUM ION
Molecular weight formula_weight	39.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	344

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1dhpa_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.10 — Aldolase
Family Family family	c.1.10.1 — Class I aldolase

Domain ID domain_id	d1dhpb_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.10 — Aldolase
Family Family family	c.1.10.1 — Class I aldolase

CATH v4.4 (2 domains)

Domain ID domain_id	1dhpA00
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	1dhpB00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	70 — Aldolase class I

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8. Citations (2)

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Unit-cell length a length_a	122.410 Å
Unit-cell length b length_b	122.410 Å
Unit-cell length c length_c	111.220 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	12

Space group space_group	P 31 2 1
Space-group number int_tables_number	152
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.1970
R_work r_work	0.1970
R_free r_free	—

fit	/app/data/saxs_computation/dh/1dhp/1dhp.fit
pddf	/app/data/pr_computation/dh/1dhp/1dhp.pr.out
profile	/app/data/saxs_computation/dh/1dhp/1dhp.dat

DIHYDRODIPICOLINATE SYNTHASE

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

DIHYDRODIPICOLINATE SYNTHASE

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

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)