SAXSdb — 2kqc

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

Aprataxin and PNK-like factor

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 368–451	Fragment：sequence database residues 368-451, PBZ-type 2 domain	ZN ZINC ION × 1	SOLUTION NMR NMR measurement conditions：pH 6；300 K；Ionic strength (raw mmCIF value) 0.4；Pressure ambient NMR sample composition：20 mM potassium pyrophosphate, 200 mM sodium chloride, 100 uM zinc sulphate, 2 mM [U-2H] DTT, 0.5-0.6 mM [U-98% 13C; U-98% 15N] APLF_363-451, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition：20 mM potassium pyrophosphate, 200 mM sodium chloride, 100 uM zinc sulphate, 2 mM [U-2H] DTT, 0.5-0.6 mM [U-98% 13C; U-98% 15N] APLF_363-451, 100% D2O \| 100% D2O	Resolution not provided

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 2KQC	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2KQB First PBZ domain of human APLF protein Deposited 2009-11-04	Different construct	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 368–451（84 aa） Fragment：sequence database residues 363-451, PBZ-type 1 domain	Not recorded	ZN ZINC ION × 1	SOLUTION NMR NMR measurement conditions pH 6；300 K；Ionic strength (raw mmCIF value) 0.4；Pressure ambient NMR sample composition 20 mM potassium pyrophosphate, 200 mM sodium chloride, 100 uM zinc sulphate, 2 mM [U-2H] DTT, 0.5-0.6 mM [U-98% 13C; U-98% 15N] APLF_363-451, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 20 mM potassium pyrophosphate, 200 mM sodium chloride, 100 uM zinc sulphate, 2 mM [U-2H] DTT, 0.5-0.6 mM [U-98% 13C; U-98% 15N] APLF_363-451, 100% D2O \| 100% D2O	Resolution not provided
2KQD First PBZ domain of human APLF protein in complex with ribofuranosyladenosine Deposited 2009-11-04	Different construct Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 368–451（84 aa） Fragment：sequence database residues 363-451, PBZ-type 1 domain	Not recorded	ZN ZINC ION × 1 ADN ADENOSINE × 1 RIB alpha-D-ribofuranose × 1	SOLUTION NMR NMR measurement conditions pH 6；278 K；Ionic strength (raw mmCIF value) 0.4；Pressure ambient NMR measurement conditions pH 6；286 K；Ionic strength (raw mmCIF value) 0.4；Pressure ambient NMR measurement conditions pH 6；300 K；Ionic strength (raw mmCIF value) 0.4；Pressure ambient NMR sample composition 20 mM potassium pyrophosphate, 200 mM sodium chloride, 100 uM zinc sulphate, 2 mM [U-2H] DTT, 0.8 mM [U-98% 13C; U-98% 15N] APLF_363-451, 2 mM RFA, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 20 mM potassium pyrophosphate, 200 mM sodium chloride, 100 uM zinc sulphate, 2 mM [U-2H] DTT, 0.8 mM [U-98% 13C; U-98% 15N] APLF_363-451, 2 mM RFA, 100% D2O \| 100% D2O	Resolution not provided
2KQE Second PBZ domain of human APLF protein in complex with ribofuranosyladenosine Deposited 2009-11-04	Different construct Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 368–451（84 aa） Fragment：sequence database residues 363-451, PBZ-type 2 domain	Not recorded	ZN ZINC ION × 1 ADN ADENOSINE × 1 RIB alpha-D-ribofuranose × 1	SOLUTION NMR NMR measurement conditions pH 6；278 K；Ionic strength (raw mmCIF value) 0.4；Pressure ambient NMR measurement conditions pH 6；286 K；Ionic strength (raw mmCIF value) 0.4；Pressure ambient NMR measurement conditions pH 6；300 K；Ionic strength (raw mmCIF value) 0.4；Pressure ambient NMR sample composition 20 mM potassium pyrophosphate, 200 mM sodium chloride, 100 uM zinc sulphate, 2 mM [U-2H] DTT, 0.8 mM [U-98% 13C; U-98% 15N] APLF_363-451, 2 mM RFA, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 20 mM potassium pyrophosphate, 200 mM sodium chloride, 100 uM zinc sulphate, 2 mM [U-2H] DTT, 0.8 mM [U-98% 13C; U-98% 15N] APLF_363-451, 2 mM RFA, 100% D2O \| 100% D2O	Resolution not provided
2KUO Structure and identification of ADP-ribose recognition motifs of APLF and role in the DNA damage response Deposited 2010-02-23	Different construct Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 360–448（89 aa） Fragment：APLF TZF	Not recorded	ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) 50；Pressure ambient NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 150；Pressure ambient NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) 500；Pressure ambient NMR sample composition 0.5-0.8 mM [U-100% 13C; U-100% 15N] APLF Tandem ZF, 20 mM Bis-tris, 50 mM sodium chloride, 1 mM sodium azide, 0.05 mM zinc chloride, 93% H2O/7% D2O \| 93% H2O/7% D2O NMR sample composition 0.5-0.8 mM [U-100% 13C; U-100% 15N] APLF Tandem ZF, 20 mM Bis-tris, 50 mM sodium chloride, 1 mM sodium azide, 0.05 mM zinc chloride, 99% D2O \| 99% D2O NMR sample composition 0.1 mM [U-100% 15N] APLF Tandem ZF, 20 mM Bis-tris, 50 mM sodium chloride, 1 mM sodium azide, 0.05 mM zinc chloride, 93% H2O/7% D2O \| 93% H2O/7% D2O NMR sample composition 0.1 mM [U-100% 15N] APLF Tandem ZF, 20 mM sodium phosphate, 150 mM potassium chloride, 1 mM sodium azide, 0.05 mM zinc chloride, 2 mM magnesium chloride, 93% H2O/7% D2O \| 93% H2O/7% D2O NMR sample composition 0.5 mM [U-100% 15N] APLF Tandem ZF, 20 mM Bis-tris, 500 mM sodium chloride, 1 mM sodium azide, 0.05 mM zinc chloride, 10 mg/mL Pf1 phage, 93% H2O/7% D2O \| 93% H2O/7% D2O	Resolution not provided
5E50 APLF/XRCC4 complex Deposited 2015-10-07	Different construct 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 A 1–105（105 aa）	Not recorded	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Protein complex at 10 mg/ml, in 50 mM HEPES pH 7.5, 150 mM NaCl, 5 mM beta-mercaptoethanol. The complex crystallised from hanging drops set up at 18 oC with equal volumes of protein and reservoir solution 0.1M Tris pH 8.0, 30% w/v PEG 3350, 0.2M MgCl2.	Resolution 1.38 Å R-free 0.174
5E50 APLF/XRCC4 complex Deposited 2015-10-07	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–105（105 aa）	Not recorded	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Protein complex at 10 mg/ml, in 50 mM HEPES pH 7.5, 150 mM NaCl, 5 mM beta-mercaptoethanol. The complex crystallised from hanging drops set up at 18 oC with equal volumes of protein and reservoir solution 0.1M Tris pH 8.0, 30% w/v PEG 3350, 0.2M MgCl2.	Resolution 1.38 Å R-free 0.174
5W7W Crystal Structure of FHA domain of human APLF Deposited 2017-06-21	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain T 1–105（105 aa） Fragment：UNP residues 1-105	Not recorded	FMT FORMIC ACID × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；3.5M sodium formate	Resolution 1.35 Å R-free 0.164
5W7W Crystal Structure of FHA domain of human APLF Deposited 2017-06-21	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–105（105 aa） Fragment：UNP residues 1-105	Not recorded	FMT FORMIC ACID × 1 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；3.5M sodium formate	Resolution 1.35 Å R-free 0.164
5W7X Crystal Structure of FHA domain of human APLF in complex with XRCC1 bisphospho peptide Deposited 2017-06-21	Different construct 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 D 1–105（105 aa） Fragment：UNP residues 1-105	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.6mM XRCC1 bisphosphopeptide 0.6mM APLF 0.5M lithium chloride 0.1M Tris 28% PEG 6000	Resolution 2.00 Å R-free 0.229
5W7X Crystal Structure of FHA domain of human APLF in complex with XRCC1 bisphospho peptide Deposited 2017-06-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–105（105 aa） Fragment：UNP residues 1-105	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.6mM XRCC1 bisphosphopeptide 0.6mM APLF 0.5M lithium chloride 0.1M Tris 28% PEG 6000	Resolution 2.00 Å R-free 0.229
5W7X Crystal Structure of FHA domain of human APLF in complex with XRCC1 bisphospho peptide Deposited 2017-06-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–105（105 aa） Fragment：UNP residues 1-105	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.6mM XRCC1 bisphosphopeptide 0.6mM APLF 0.5M lithium chloride 0.1M Tris 28% PEG 6000	Resolution 2.00 Å R-free 0.229
5W7X Crystal Structure of FHA domain of human APLF in complex with XRCC1 bisphospho peptide Deposited 2017-06-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–105（105 aa） Fragment：UNP residues 1-105	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.6mM XRCC1 bisphosphopeptide 0.6mM APLF 0.5M lithium chloride 0.1M Tris 28% PEG 6000	Resolution 2.00 Å R-free 0.229
5W7Y Crystal Structure of FHA domain of human APLF in complex with XRCC1 monophosphorylated mutated peptide Deposited 2017-06-21	Different construct 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 A 1–105（105 aa） Fragment：UNP residues 1-105	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.6mM APLF 0.6mM XRCC1 peptide 0.1M Tris 30% PEG 1000	Resolution 2.10 Å R-free 0.237
5W7Y Crystal Structure of FHA domain of human APLF in complex with XRCC1 monophosphorylated mutated peptide Deposited 2017-06-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–105（105 aa） Fragment：UNP residues 1-105	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.6mM APLF 0.6mM XRCC1 peptide 0.1M Tris 30% PEG 1000	Resolution 2.10 Å R-free 0.237
6ERF Complex of APLF factor and Ku heterodimer bound to DNA Deposited 2017-10-18	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: pentameric	Chain Q 174–191（18 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；100 mM Bris Tris propane 13% PEG 3350 150 mM Na nirate	Resolution 3.01 Å R-free 0.227
6ERF Complex of APLF factor and Ku heterodimer bound to DNA Deposited 2017-10-18	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–DNA Heteromer；Protein × 3 PDB declaration: pentameric	Chain R 174–191（18 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；100 mM Bris Tris propane 13% PEG 3350 150 mM Na nirate	Resolution 3.01 Å R-free 0.227
6ERF Complex of APLF factor and Ku heterodimer bound to DNA Deposited 2017-10-18	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein–DNA Heteromer；Protein × 3 PDB declaration: pentameric	Chain S 174–191（18 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；100 mM Bris Tris propane 13% PEG 3350 150 mM Na nirate	Resolution 3.01 Å R-free 0.227
6ERF Complex of APLF factor and Ku heterodimer bound to DNA Deposited 2017-10-18	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein–DNA Heteromer；Protein × 3 PDB declaration: pentameric	Chain T 174–191（18 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；100 mM Bris Tris propane 13% PEG 3350 150 mM Na nirate	Resolution 3.01 Å R-free 0.227
6YN1 Crystal structure of histone chaperone APLF acidic domain bound to the histone H2A-H2B-H3-H4 octamer Deposited 2020-04-10	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 × 10 PDB declaration: decameric	Chain E 449–490（42 aa） Chain J 449–490（42 aa）	Not recorded	GOL GLYCEROL × 3 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate	Resolution 2.35 Å R-free 0.233
6YN1 Crystal structure of histone chaperone APLF acidic domain bound to the histone H2A-H2B-H3-H4 octamer Deposited 2020-04-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain O 449–490（42 aa） Chain T 449–490（42 aa）	Not recorded	GOL GLYCEROL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate	Resolution 2.35 Å R-free 0.233
6YN1 Crystal structure of histone chaperone APLF acidic domain bound to the histone H2A-H2B-H3-H4 octamer Deposited 2020-04-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain Y 449–490（42 aa） Chain d 449–490（42 aa）	Not recorded	GOL GLYCEROL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate	Resolution 2.35 Å R-free 0.233
6YN1 Crystal structure of histone chaperone APLF acidic domain bound to the histone H2A-H2B-H3-H4 octamer Deposited 2020-04-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain i 449–490（42 aa） Chain n 449–490（42 aa）	Not recorded	GOL GLYCEROL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate	Resolution 2.35 Å R-free 0.233

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

View Construct and Data Evidence

UniProt name	APLF_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 6–89； UniProt 368–451

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	2kqc
Deposition date deposition_date	2009-11-04
Structure title title	Second PBZ domain of human APLF protein
Keywords keywords	ADP-ribosylation, DNA damage, DNA repair, Metal-binding, Nucleotide-binding, Nucleus, Zinc, Zinc-finger, LYASE; LYASE
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	13.11 Å
Radius of gyration Rg (electron density) rg_electron	13.41 Å
Forward intensity I(0) i0	330401000.00
Molecular weight molecular_weight	137210.0 kDa
Excluded volume excluded_volume	165210 Å³
Envelope volume envelope_volume	34039 Å³
Hydration-shell volume shell_volume	16138 Å³
Envelope diameter envelope_diameter	55.4 Å
Shell Rg shell_rg	23.84 Å
Envelope Rg envelope_rg	18.53 Å
Shape Rg shape_rg	13.42 Å
Total Rg total_rg	13.71 Å
Total atoms total_atoms	18425
Residues n_residues	1175
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	50.5 Å
Rg (real space) rg_real	13.24 Å
Rg uncertainty (real space) rg_real_error	0.43 Å
I(0) (real space) i0_real	3.3040e+08
I(0) uncertainty (real space) i0_real_error	3.9780e+06
Rg (reciprocal space) rg_reciprocal	13.23 Å
I(0) (reciprocal space) i0_reciprocal	330400000.0000
Solution quality estimate total_estimate	0.5311
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	12.1 Å
Skewness Skewness skewness	0.473
Kurtosis Kurtosis kurtosis	-0.365
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	87050.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.620; Stabil: 1.000; Sysdev: 0.256; Positv: 1.000; Valcen: 0.270; 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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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

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

Description description	Aprataxin and PNK-like factor
Molecular weight formula_weight	10053.1 kDa
EC 编号 ec_number	4.2.99.18
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	18425

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

Second PBZ domain of human APLF protein

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

Aprataxin and PNK-like factor

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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

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

fit	/app/data/saxs_computation/kq/2kqc/2kqc.fit
pddf	/app/data/pr_computation/kq/2kqc/2kqc.pr.out
profile	/app/data/saxs_computation/kq/2kqc/2kqc.dat