SAXSdb — 2lnh

▼

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

Neural Wiskott-Aldrich syndrome protein

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 207–270	Fragment：UNP residues 207-270	Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1 × 1 （Q9UHR4） Secreted effector protein EspF(U) × 1 （P0DJ89）	SOLUTION NMR NMR measurement conditions：pH 7；298 K；Ionic strength (raw mmCIF value) 50；Pressure ambient NMR sample composition：0.3 mM [U-98% 13C; U-98% 15N] protein_1, 0.3 mM protein_2, 0.3 mM protein_3, 93% H2O/7% D2O \| 93% H2O/7% D2O NMR sample composition：0.5 mM protein_1, 0.5 mM [U-98% 13C; U-98% 15N] protein_2, 0.5 mM protein_3, 93% H2O/7% D2O \| 93% H2O/7% D2O NMR sample composition：0.5 mM protein_1, 0.5 mM protein_2, 0.5 mM [U-98% 13C; U-98% 15N] protein_3, 93% H2O/7% D2O \| 93% H2O/7% 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 2LNH	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2FF3 Crystal structure of Gelsolin domain 1:N-wasp V2 motif hybrid in complex with actin Deposited 2005-12-19	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 451–465（15 aa） Fragment：N-wasp second WH2 domain	Not recorded	CA CALCIUM ION × 3 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions MICROBATCH；pH 6.5；293.15 K；5% PEG 8000, 0.1M sodium acetate, 10mM calcium chloride, pH 6.5, microbatch, temperature 293.15K	Resolution 2.00 Å R-free 0.250
2VCP Crystal structure of N-Wasp VC domain in complex with skeletal actin Deposited 2007-09-26	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 392–484（93 aa） Fragment：WH2 1,2 AND C DOMAIN, RESIDUES 392-484	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7；277 K；VAPOR DIFFUSION METHOD (4 C) PROTEIN SOLUTION: 0.18MM ACTIN, 0.36MM N-WASP PEPTIDE, 5MM TRIS.HCL PH7.0, ATP 0.2MM, CACL2 0.02MM, TCEP 20MM, NAN3 0.01%. RESERVOIR: 10.2% (V/V) TACSIMATE, 13.2%(W/V)PEG 8000, 100MM HEPES PH7.0	Resolution 3.20 Å R-free 0.331
2VCP Crystal structure of N-Wasp VC domain in complex with skeletal actin Deposited 2007-09-26	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 E 392–484（93 aa） Fragment：WH2 1,2 AND C DOMAIN, RESIDUES 392-484	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7；277 K；VAPOR DIFFUSION METHOD (4 C) PROTEIN SOLUTION: 0.18MM ACTIN, 0.36MM N-WASP PEPTIDE, 5MM TRIS.HCL PH7.0, ATP 0.2MM, CACL2 0.02MM, TCEP 20MM, NAN3 0.01%. RESERVOIR: 10.2% (V/V) TACSIMATE, 13.2%(W/V)PEG 8000, 100MM HEPES PH7.0	Resolution 3.20 Å R-free 0.331
4CC2 Complex of human Tuba C-terminal SH3 domain with human N-WASP proline- rich peptide - P212121 Deposited 2013-10-17	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 B 346–357（12 aa） Fragment：N-WASP PROLINE-RICH PEPTIDE, RESIDUES 346-357	Not recorded	GOL GLYCEROL × 3 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；3 M NACL, 0.1 M BIS-TRIS PH 5.5	Resolution 1.55 Å R-free 0.218
4CC2 Complex of human Tuba C-terminal SH3 domain with human N-WASP proline- rich peptide - P212121 Deposited 2013-10-17	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 D 346–357（12 aa） Fragment：N-WASP PROLINE-RICH PEPTIDE, RESIDUES 346-357	Not recorded	GOL GLYCEROL × 1 CL CHLORIDE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；3 M NACL, 0.1 M BIS-TRIS PH 5.5	Resolution 1.55 Å R-free 0.218
4CC7 Crystal structure of the sixth or C-terminal SH3 domain of human Tuba in complex with proline-rich peptides of N-WASP. Space group P41 Deposited 2013-10-18	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 B 346–357（12 aa） Fragment：PROLINE-RICH REGION, RESIDUES 346-357	Not recorded	GOL GLYCEROL × 1 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；3 M NACL, 0.1 M BIS-TRIS PH 5.5	Resolution 1.97 Å R-free 0.215
4CC7 Crystal structure of the sixth or C-terminal SH3 domain of human Tuba in complex with proline-rich peptides of N-WASP. Space group P41 Deposited 2013-10-18	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 D 346–357（12 aa） Fragment：PROLINE-RICH REGION, RESIDUES 346-357	Not recorded	GOL GLYCEROL × 1 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；3 M NACL, 0.1 M BIS-TRIS PH 5.5	Resolution 1.97 Å R-free 0.215
4CC7 Crystal structure of the sixth or C-terminal SH3 domain of human Tuba in complex with proline-rich peptides of N-WASP. Space group P41 Deposited 2013-10-18	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 F 346–357（12 aa） Fragment：PROLINE-RICH REGION, RESIDUES 346-357	Not recorded	CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；3 M NACL, 0.1 M BIS-TRIS PH 5.5	Resolution 1.97 Å R-free 0.215
4CC7 Crystal structure of the sixth or C-terminal SH3 domain of human Tuba in complex with proline-rich peptides of N-WASP. Space group P41 Deposited 2013-10-18	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 H 346–357（12 aa） Fragment：PROLINE-RICH REGION, RESIDUES 346-357	Not recorded	CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；3 M NACL, 0.1 M BIS-TRIS PH 5.5	Resolution 1.97 Å R-free 0.215
4CC7 Crystal structure of the sixth or C-terminal SH3 domain of human Tuba in complex with proline-rich peptides of N-WASP. Space group P41 Deposited 2013-10-18	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain J 346–357（12 aa） Fragment：PROLINE-RICH REGION, RESIDUES 346-357	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；3 M NACL, 0.1 M BIS-TRIS PH 5.5	Resolution 1.97 Å R-free 0.215
4CC7 Crystal structure of the sixth or C-terminal SH3 domain of human Tuba in complex with proline-rich peptides of N-WASP. Space group P41 Deposited 2013-10-18	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 346–357（12 aa） Fragment：PROLINE-RICH REGION, RESIDUES 346-357	Not recorded	GOL GLYCEROL × 1 CL CHLORIDE ION × 3 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；3 M NACL, 0.1 M BIS-TRIS PH 5.5	Resolution 1.97 Å R-free 0.215
4CC7 Crystal structure of the sixth or C-terminal SH3 domain of human Tuba in complex with proline-rich peptides of N-WASP. Space group P41 Deposited 2013-10-18	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 7 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain N 346–357（12 aa） Fragment：PROLINE-RICH REGION, RESIDUES 346-357	Not recorded	GOL GLYCEROL × 1 CL CHLORIDE ION × 4 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；3 M NACL, 0.1 M BIS-TRIS PH 5.5	Resolution 1.97 Å R-free 0.215
9DLX Bovine Arp2/3 complex with N-WASP CA bound to Arp3 and Arp2-ArpC1 Deposited 2024-09-11	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 × 9 PDB declaration: nonameric	Chain H 465–505（41 aa） Chain I 465–505（41 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.91 Å
9R3Y Solution NMR structure of N-WASP GBD in complex with EspFu R5 Deposited 2025-05-06	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 207–275（69 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 0.11；Pressure ambient NMR sample composition 0.5 mM [U-13C; U-15N] N-WASP GBD, 0.6 mM EspFu R5, 20 mM sodium phosphate, 50 mM sodium chloride, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.4 mM N-WASP GBD, 0.3 mM [U-13C; U-15N] EspFu R5, 20 mM sodium phosphate, 50 mM sodium chloride, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
9R4V Solution structure of N-WASP GBD in complex with EspF Deposited 2025-05-08	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 207–275（69 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 0.1；Pressure ambient NMR sample composition 0.5 mM [U-13C; U-15N] N-WASP GBD, 0.6 mM EspF, 20 mM sodium phosphate, 50 mM sodium chloride, 93% H2O/7% D2O \| 93% H2O/7% D2O NMR sample composition 0.7 mM GBD, 0.5 mM [U-13C; U-15N] EspF, 20 mM sodium phosphate, 50 mM sodium chloride, 93% H2O/7% D2O \| 93% H2O/7% D2O	Resolution not provided

7 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	WASL_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–65； UniProt 207–270

Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1

Homo sapiens

UniProt Q9UHR4

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain B； UniProt 339–402	Fragment：SH3 domain residues 339-402	Neural Wiskott-Aldrich syndrome protein × 1 （O00401） Secreted effector protein EspF(U) × 1 （P0DJ89）	SOLUTION NMR NMR measurement conditions：pH 7；298 K；Ionic strength (raw mmCIF value) 50；Pressure ambient NMR sample composition：0.3 mM [U-98% 13C; U-98% 15N] protein_1, 0.3 mM protein_2, 0.3 mM protein_3, 93% H2O/7% D2O \| 93% H2O/7% D2O NMR sample composition：0.5 mM protein_1, 0.5 mM [U-98% 13C; U-98% 15N] protein_2, 0.5 mM protein_3, 93% H2O/7% D2O \| 93% H2O/7% D2O NMR sample composition：0.5 mM protein_1, 0.5 mM protein_2, 0.5 mM [U-98% 13C; U-98% 15N] protein_3, 93% H2O/7% D2O \| 93% H2O/7% 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 2LNH	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2KXC 1H, 13C, and 15N Chemical Shift Assignments for IRTKS-SH3 and EspFu-R47 complex Deposited 2010-04-30	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 339–402（64 aa） Fragment：IRTKS-SH3 domain, UNP residues 339-402	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 50；Pressure AMBIENT NMR sample composition 0.48 mM [U-98% 13C; U-98% 15N] IRTKS-SH3-1, 0.48 mM EspFu-R47-2, 93% H2O/7% D2O \| 93% H2O/7% D2O NMR sample composition 0.9 mM [U-98% 13C; U-98% 15N] EspFu-R47-3, 0.9 mM IRTKS-SH3-4, 93% H2O/7% D2O \| 93% H2O/7% D2O	Resolution not provided

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	BI2L1_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 4–67； UniProt 339–402

Secreted effector protein EspF(U)

Escherichia coli O157:H7

UniProt P0DJ89

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain C； UniProt 221–267	Fragment：UNP residues 221-267	Neural Wiskott-Aldrich syndrome protein × 1 （O00401） Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1 × 1 （Q9UHR4）	SOLUTION NMR NMR measurement conditions：pH 7；298 K；Ionic strength (raw mmCIF value) 50；Pressure ambient NMR sample composition：0.3 mM [U-98% 13C; U-98% 15N] protein_1, 0.3 mM protein_2, 0.3 mM protein_3, 93% H2O/7% D2O \| 93% H2O/7% D2O NMR sample composition：0.5 mM protein_1, 0.5 mM [U-98% 13C; U-98% 15N] protein_2, 0.5 mM protein_3, 93% H2O/7% D2O \| 93% H2O/7% D2O NMR sample composition：0.5 mM protein_1, 0.5 mM protein_2, 0.5 mM [U-98% 13C; U-98% 15N] protein_3, 93% H2O/7% D2O \| 93% H2O/7% 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	ESFU3_ECO57
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 2–48； UniProt 221–267

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	2lnh
Deposition date deposition_date	2011-12-28
Structure title title	Enterohaemorrhagic E. coli (EHEC) exploits a tryptophan switch to hijack host F-actin assembly
Keywords keywords	Protein complex, Signaling Protein-Protein Binding complex; Signaling Protein/Protein Binding
Experimental Method method	SOLUTION NMR

▼

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

Radius of gyration Rg (Guinier) rg_guinier	23.99 Å
Radius of gyration Rg (electron density) rg_electron	23.60 Å
Forward intensity I(0) i0	2276750000.00
Molecular weight molecular_weight	399690.0 kDa
Excluded volume excluded_volume	498520 Å³
Envelope volume envelope_volume	157170 Å³
Hydration-shell volume shell_volume	41142 Å³
Envelope diameter envelope_diameter	113.1 Å
Shell Rg shell_rg	38.36 Å
Envelope Rg envelope_rg	32.98 Å
Shape Rg shape_rg	23.64 Å
Total Rg total_rg	23.82 Å
Total atoms total_atoms	55640
Residues n_residues	3580
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

▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	63.5 Å
Rg (real space) rg_real	22.60 Å
Rg uncertainty (real space) rg_real_error	0.11 Å
I(0) (real space) i0_real	2.1690e+09
I(0) uncertainty (real space) i0_real_error	2.0460e+07
Rg (reciprocal space) rg_reciprocal	24.16 Å
I(0) (reciprocal space) i0_reciprocal	2277000000.0000
Solution quality estimate total_estimate	0.6831
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	21.9 Å
Skewness Skewness skewness	0.288
Kurtosis Kurtosis kurtosis	-0.661
Angular range angular_range	— – 0.3300 Å⁻¹
Current regularization parameter α current_alpha	2.6620
Highest regularization parameter α highest_alpha	6011000.0000
Real-space data points n_real_points	65
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.001; Oscil: 0.987; Stabil: 0.984; Sysdev: 0.000; Positv: 1.000; Valcen: 0.969; Smooth: 0.000

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Neural Wiskott-Aldrich syndrome protein
Molecular weight formula_weight	7262.0 kDa
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	55640

GSNFQHIGHVGWDPNTGFDLNNLDPELKNLFDMCGISEAQLKDRETSKVIYDFIEKTGGVEAVKN

来源 Source

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

Entity 2 Entity 2 polymer

Description description	Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1
Molecular weight formula_weight	7559.6 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

GSHMKKQKVKTIFPHTAGSNKTLLSFAQGDVITLLIPEEKDGWLYGEHDVSKARGWFPSSYTKLLEE

来源 Source

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

Entity 3 Entity 3 polymer

Description description	Secreted effector protein EspF(U)
Molecular weight formula_weight	5302.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

GLPDVAQRLMQHLAEHGIQPARNMAEHIPPAPNWPAPTPPVQNEQSRP

来源 Source

来源生物 organism	Escherichia coli O157:H7
NCBI Class编号 ncbi_taxonomy_id	83334
宿主生物 host_organism	Escherichia coli

▼

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2lnhb1
Class class	b — All beta proteins
Fold Fold fold	b.34 — SH3-like barrel
Superfamily Superfamily superfamily	b.34.2 — SH3-domain
Family Family family	b.34.2.1 — SH3-domain

Domain ID domain_id	d2lnhb2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (3 domains)

Domain ID domain_id	2lnhA00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	810 — SerineThreonine-protein kinase PAK-alpha; Chain A
Homologous superfamily homologous superfamily	10 — CRIB domain

Domain ID domain_id	2lnhB00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	30 — SH3 type barrels.
Homologous superfamily homologous superfamily	40 — SH3 Domains

Domain ID domain_id	2lnhC00
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	3330 — TccP2/EspF(U)-like

▶

8. Citations (1)

▶

fit	/app/data/saxs_computation/ln/2lnh/2lnh.fit
pddf	/app/data/pr_computation/ln/2lnh/2lnh.pr.out
profile	/app/data/saxs_computation/ln/2lnh/2lnh.dat

Enterohaemorrhagic E. coli (EHEC) exploits a tryptophan switch to hijack host F-actin assembly

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

Neural Wiskott-Aldrich syndrome protein

State in the Current Structure

Other States of the Same Protein in the Database

Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1

State in the Current Structure

Other States of the Same Protein in the Database

Secreted effector protein EspF(U)

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

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

CATH v4.4 (3 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)