SAXSdb — 1dpi

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

DNA POLYMERASE I KLENOW FRAGMENT

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 324–928	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.80 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 1DPI	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1D8Y CRYSTAL STRUCTURE OF THE COMPLEX OF DNA POLYMERASE I KLENOW FRAGMENT WITH DNA Deposited 1999-10-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: dimeric	Chain A 324–928（605 aa） Fragment：KLENOW FRAGMENT	Mutation：D355A, E357A	ZN ZINC ION × 1 SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；295 K；SODIUM CITRATE, pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 2.08 Å R-free 0.233
1KFD CRYSTAL STRUCTURES OF THE KLENOW FRAGMENT OF DNA POLYMERASE I COMPLEXED WITH DEOXYNUCLEOSIDE TRIPHOSPHATE AND PYROPHOSPHATE Deposited 1993-09-23	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 324–928（605 aa）	Not recorded	CTP CYTIDINE-5'-TRIPHOSPHATE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.90 Å
1KFS DNA POLYMERASE I KLENOW FRAGMENT (E.C.2.7.7.7) MUTANT/DNA COMPLEX Deposited 1997-08-18	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: dimeric	Chain A 324–928（605 aa）	Mutation：V324M	MG MAGNESIUM ION × 1 ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.8；1.4 M NA CITRATE PH 5.8	Resolution 2.10 Å R-free 0.219
1KLN DNA POLYMERASE I KLENOW FRAGMENT (E.C.2.7.7.7) MUTANT/DNA COMPLEX Deposited 1994-05-24	Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: trimeric	Chain A 324–928（605 aa）	Mutation：D355A	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.8；290 K；pH 6.80, VAPOR DIFFUSION, temperature 290.00K	Resolution 3.20 Å
1KRP DNA polymerase I Klenow fragment (E.C.2.7.7.7) mutant/DNA complex Deposited 1997-08-19	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: dimeric	Chain A 324–928（605 aa）	Mutation：V324M	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.8；1.4 M NA CITRATE PH 5.8	Resolution 2.20 Å R-free 0.255
1KSP DNA polymerase I Klenow fragment (E.C.2.7.7.7) mutant/DNA complex Deposited 1997-08-19	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: dimeric	Chain A 324–928（605 aa）	Mutation：V324M	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.8；1.4 M NA CITRATE PH 5.8	Resolution 2.30 Å R-free 0.241
1QSL KLENOW FRAGMENT COMPLEXED WITH SINGLE-STRANDED SUBSTRATE AND EUROPIUM (III) ION Deposited 1999-06-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: dimeric	Chain A 324–928（605 aa） Fragment：KLENOW FRAGMENT	Mutation：V324M	EU EUROPIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；290 K；1.5 M SODIUM CITRATE AT 290 K, pH 5.60, VAPOR DIFFUSION, HANGING DROP	Resolution 2.20 Å R-free 0.255
2KFN KLENOW FRAGMENT WITH BRIDGING-SULFUR SUBSTRATE AND MANGANESE Deposited 1998-07-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: dimeric	Chain A 325–928（604 aa） Fragment：LARGE FRAGMENT, KLENOW FRAGMENT	Mutation：V324M	MN MANGANESE (II) ION × 1 ZN ZINC ION × 3 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.8；1.4 M NA CITRATE PH 5.8	Resolution 2.03 Å R-free 0.250
2KFZ KLENOW FRAGMENT WITH BRIDGING-SULFUR SUBSTRATE AND ZINC ONLY Deposited 1998-07-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: dimeric	Chain A 325–928（604 aa） Fragment：LARGE FRAGMENT, KLENOW FRAGMENT	Mutation：V324M	ZN ZINC ION × 4 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.8；1.4 M NA CITRATE PH 5.8	Resolution 2.03 Å R-free 0.255
2KZM KLENOW FRAGMENT WITH NORMAL SUBSTRATE AND ZINC AND MANGANESE Deposited 1998-07-03	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: dimeric	Chain A 324–928（605 aa） Fragment：KLENOW FRAGMENT, LARGE FRAGMENT	Not recorded	MN MANGANESE (II) ION × 1 ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；1.4 M SODIUM CITRATE PH 5.8, pH 5.5, VAPOR DIFFUSION, HANGING DROP	Resolution 2.60 Å R-free 0.243
2KZZ KLENOW FRAGMENT WITH NORMAL SUBSTRATE AND ZINC ONLY Deposited 1998-07-07	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: dimeric	Chain A 324–928（605 aa） Fragment：KLENOW FRAGMENT, LARGE FRAGMENT	Not recorded	ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；1.4 M SODIUM CITRATE PH 5.8, pH 5.5, VAPOR DIFFUSION, HANGING DROP	Resolution 2.25 Å R-free 0.251
8OO6 Pol I bound to extended and displaced DNA section - closed conformation Deposited 2023-04-04	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: tetrameric	Chain A 328–928（601 aa）	Not recorded	MG MAGNESIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.30 Å
8OOY Pol I bound to extended and displaced DNA section - open conformation Deposited 2023-04-06	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: tetrameric	Chain A 328–928（601 aa）	Not recorded	MG MAGNESIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.00 Å

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	DPO1_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–605； UniProt 324–928

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	1dpi
Deposition date deposition_date	1987-08-11
Structure title title	STRUCTURE OF LARGE FRAGMENT OF ESCHERICHIA COLI DNA POLYMERASE I COMPLEXED WITH D/TMP
Keywords keywords	NUCLEOTIDYLTRANSFERASE; NUCLEOTIDYLTRANSFERASE
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	26.51 Å
Radius of gyration Rg (electron density) rg_electron	26.16 Å
Forward intensity I(0) i0	59847300.00
Molecular weight molecular_weight	61609.0 kDa
Excluded volume excluded_volume	75696 Å³
Envelope volume envelope_volume	59786 Å³
Hydration-shell volume shell_volume	21423 Å³
Envelope diameter envelope_diameter	86.5 Å
Shell Rg shell_rg	30.02 Å
Envelope Rg envelope_rg	24.45 Å
Shape Rg shape_rg	26.14 Å
Total Rg total_rg	26.47 Å
Total atoms total_atoms	1
Residues n_residues	—
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	82.2 Å
Rg (real space) rg_real	26.46 Å
Rg uncertainty (real space) rg_real_error	0.36 Å
I(0) (real space) i0_real	5.9850e+07
I(0) uncertainty (real space) i0_real_error	7.8800e+05
Rg (reciprocal space) rg_reciprocal	26.48 Å
I(0) (reciprocal space) i0_reciprocal	59850000.0000
Solution quality estimate total_estimate	0.9091
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	79.5 Å
Skewness Skewness skewness	0.275
Kurtosis Kurtosis kurtosis	-0.349
Angular range angular_range	— – 0.3000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	8708000.0000
Real-space data points n_real_points	61
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.948; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.970

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	DNA POLYMERASE I KLENOW FRAGMENT
Molecular weight formula_weight	68161.7 kDa
EC 编号 ec_number	2.7.7.7
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	547

VISYDNYVTILDEETLKAWIAKLEKAPVFAFDTETDSLDNISANLVGLSFAIEPGVAAYIPVAHDYLDAPDQISRERALELLKPLLEDEKALKVGQNLKYDRGILANYGIELRGIAFDTMLESYILNSVAGRHDMDSLAERWLKHKTITFEEIAGKGKNQLTFNQIALEEAGRYAAEDADVTLQLHLKMWPDLQKHKGPLNVFENIEMPLVPVLSRIERNGVKIDPKVLHNHSEELTLRLAELEKKAHEIAGEEFNLSSTKQLQTILFEKQGIKPLKKTPGGAPSTSEEVLEELALDYPLPKVILEYRGLAKLKSTYTDKLPLMINPKTGRVHTSYHQAVTATGRLSSTDPNLQNIPVRNEEGRRIRQAFIAPEDYVIVSADYSQIELRIMAHLSRDKGLLTAFAEGKDIHRATAAEVFGLPLETVTSEQRRSAKAINFGLIYGMSAFGLARQLNIPRKEAQKYMDLYFERYPGVLEYMERTRAQAKEQGYVETLDGRRLYLPDIKSSNGARRAAAERAAINAPMQGTAADIIKRAMIAVDAWLQAEQPRVRMIMQVHDELVFEVHKDDVDAVAKQIHQLMENCTRLDVPLLVEVGSGENWDQAH

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562

Entity 2 Entity 2 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	1

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1dpia1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamily	c.55.3 — Ribonuclease H-like
Family Family family	c.55.3.5 — DnaQ-like 3'-5' exonuclease

Domain ID domain_id	d1dpia2
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.8 — DNA/RNA polymerases
Superfamily Superfamily superfamily	e.8.1 — DNA/RNA polymerases
Family Family family	e.8.1.1 — DNA polymerase I

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8. Citations (5)

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Unit-cell length a length_a	102.900 Å
Unit-cell length b length_b	102.900 Å
Unit-cell length c length_c	85.800 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 43
Space-group number int_tables_number	78
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	0.2000
R_work r_work	—
R_free r_free	—

fit	/app/data/saxs_computation/dp/1dpi/1dpi.fit
pddf	/app/data/pr_computation/dp/1dpi/1dpi.pr.out
profile	/app/data/saxs_computation/dp/1dpi/1dpi.dat

STRUCTURE OF LARGE FRAGMENT OF ESCHERICHIA COLI DNA POLYMERASE I COMPLEXED WITH D/TMP

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

DNA POLYMERASE I KLENOW FRAGMENT

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