SAXSdb — 2emt

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

Radixin

Mus musculus

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 1–310	Fragment：N-terminal FERM domain (residues 1-310)	P-selectin glycoprotein ligand 1 × 2 （Q62170）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.2；277 K；8% PEG 8000, 0.1M Tris-HCl, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.294
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 1–310	Fragment：N-terminal FERM domain (residues 1-310)	P-selectin glycoprotein ligand 1 × 1 （Q62170）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.2；277 K；8% PEG 8000, 0.1M Tris-HCl, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.294

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 2EMT	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1GC6 CRYSTAL STRUCTURE OF THE RADIXIN FERM DOMAIN COMPLEXED WITH INOSITOL-(1,4,5)-TRIPHOSPHATE Deposited 2000-07-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–297（297 aa） Fragment：FERM DOMAIN	Not recorded	I3P D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；277 K；PEG 6000, MES, INOSITOL-(1,4,5)-TRIPHOSPHATE, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.90 Å R-free 0.283
1GC7 CRYSTAL STRUCTURE OF THE RADIXIN FERM DOMAIN Deposited 2000-07-21	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–297（297 aa） Fragment：FERM DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；277 K；PEG 6000, MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.255
1J19 Crystal structure of the radxin FERM domain complexed with the ICAM-2 cytoplasmic peptide Deposited 2002-12-02	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–310（310 aa） Fragment：N-terminal domain, FERM domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；277 K；PEG6000, MES, NaCl, DTT, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.40 Å R-free 0.239
2D10 Crystal structure of the Radixin FERM domain complexed with the NHERF-1 C-terminal tail peptide Deposited 2005-08-11	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–310（310 aa） Fragment：FERM domain (residues 3-312)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；10% PEG4000, 5% Isopropanol, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.50 Å R-free 0.268
2D10 Crystal structure of the Radixin FERM domain complexed with the NHERF-1 C-terminal tail peptide Deposited 2005-08-11	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–310（310 aa） Fragment：FERM domain (residues 3-312)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；10% PEG4000, 5% Isopropanol, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.50 Å R-free 0.268
2D10 Crystal structure of the Radixin FERM domain complexed with the NHERF-1 C-terminal tail peptide Deposited 2005-08-11	Different construct Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–310（310 aa） Fragment：FERM domain (residues 3-312)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；10% PEG4000, 5% Isopropanol, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.50 Å R-free 0.268
2D10 Crystal structure of the Radixin FERM domain complexed with the NHERF-1 C-terminal tail peptide Deposited 2005-08-11	Different construct Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–310（310 aa） Fragment：FERM domain (residues 3-312)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；10% PEG4000, 5% Isopropanol, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.50 Å R-free 0.268
2D11 Crystal structure of the Radixin FERM domain complexed with the NHERF-2 C-terminal tail peptide Deposited 2005-08-11	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–310（310 aa） Fragment：FERM domain (residues 1-310)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；10% PEG4000, 5% Isopropanol, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.81 Å R-free 0.278
2D11 Crystal structure of the Radixin FERM domain complexed with the NHERF-2 C-terminal tail peptide Deposited 2005-08-11	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–310（310 aa） Fragment：FERM domain (residues 1-310)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；10% PEG4000, 5% Isopropanol, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.81 Å R-free 0.278
2D11 Crystal structure of the Radixin FERM domain complexed with the NHERF-2 C-terminal tail peptide Deposited 2005-08-11	Different construct Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–310（310 aa） Fragment：FERM domain (residues 1-310)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；10% PEG4000, 5% Isopropanol, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.81 Å R-free 0.278
2D11 Crystal structure of the Radixin FERM domain complexed with the NHERF-2 C-terminal tail peptide Deposited 2005-08-11	Different construct Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–310（310 aa） Fragment：FERM domain (residues 1-310)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；10% PEG4000, 5% Isopropanol, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.81 Å R-free 0.278
2D2Q Crystal structure of the dimerized radixin FERM domain Deposited 2005-09-15	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–310（310 aa） Fragment：FERM domain (residues 1-310)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；293 K；PEG 3350, HEPES-Na, pH 7.5, VAPOR DIFFUSION, temperature 293K	Resolution 2.80 Å R-free 0.269
2D2Q Crystal structure of the dimerized radixin FERM domain Deposited 2005-09-15	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–310（310 aa） Fragment：FERM domain (residues 1-310)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；293 K；PEG 3350, HEPES-Na, pH 7.5, VAPOR DIFFUSION, temperature 293K	Resolution 2.80 Å R-free 0.269
2EMS Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule CD43 Deposited 2007-03-28	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–310（310 aa） Fragment：N-terminal FERM domain (residues 1-310)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；277 K；10% PEG 4000, 10% iso-propanol, 0.1M Sodium Citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.90 Å R-free 0.250
2YVC Crystal structure of the Radixin FERM domain complexed with the NEP cytoplasmic tail Deposited 2007-04-11	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–310（310 aa） Fragment：FERM domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277 K；20% PEG3350, 0.2M DL-maleic acid, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 3.20 Å R-free 0.267
2YVC Crystal structure of the Radixin FERM domain complexed with the NEP cytoplasmic tail Deposited 2007-04-11	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–310（310 aa） Fragment：FERM domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277 K；20% PEG3350, 0.2M DL-maleic acid, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 3.20 Å R-free 0.267
2YVC Crystal structure of the Radixin FERM domain complexed with the NEP cytoplasmic tail Deposited 2007-04-11	Different construct Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–310（310 aa） Fragment：FERM domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277 K；20% PEG3350, 0.2M DL-maleic acid, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 3.20 Å R-free 0.267
2ZPY Crystal structure of the mouse radxin FERM domain complexed with the mouse CD44 cytoplasmic peptide Deposited 2008-07-31	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–310（310 aa） Fragment：FERM domain (residues 1-310)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.6；277 K；0.1M Tris, 0.2M Potassium thiocyanate, 15% PEG 3350 , pH 8.6, VAPOR DIFFUSION, temperature 277K	Resolution 2.10 Å R-free 0.256
3X23 Radixin complex Deposited 2014-12-09	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–310（310 aa） Fragment：FERM domain, UNP reisudes 1-310	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；297 K；12% polyethylene glycol 4000, 100mM MOPS (pH 7.0), 100mM NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 297K	Resolution 2.40 Å R-free 0.237

10 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	RADI_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–312； UniProt 1–310 Author chain B； PDBConstruct 3–312； UniProt 1–310

P-selectin glycoprotein ligand 1

OrganismNot specified

UniProt Q62170

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 331–348 Chain E； UniProt 331–348	Fragment：PSGL-1 cytoplasmic peptide, 18 N-terminal residues of the cytoplasmic tail	Radixin × 1 （P26043）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.2；277 K；8% PEG 8000, 0.1M Tris-HCl, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.294
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 331–348	Fragment：PSGL-1 cytoplasmic peptide, 18 N-terminal residues of the cytoplasmic tail	Radixin × 1 （P26043）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.2；277 K；8% PEG 8000, 0.1M Tris-HCl, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.294

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	SELPL_MOUSE
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–18； UniProt 331–348 Author chain D； PDBConstruct 1–18； UniProt 331–348 Author chain E； PDBConstruct 1–18； UniProt 331–348

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	2emt
Deposition date deposition_date	2007-03-28
Structure title title	Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule PSGL-1
Keywords keywords	Protein-peptide complex, CELL ADHESION; CELL ADHESION
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	32.09 Å
Radius of gyration Rg (electron density) rg_electron	31.20 Å
Forward intensity I(0) i0	94443500.00
Molecular weight molecular_weight	78878.0 kDa
Excluded volume excluded_volume	99724 Å³
Envelope volume envelope_volume	136880 Å³
Hydration-shell volume shell_volume	36609 Å³
Envelope diameter envelope_diameter	106.2 Å
Shell Rg shell_rg	38.28 Å
Envelope Rg envelope_rg	30.58 Å
Shape Rg shape_rg	31.17 Å
Total Rg total_rg	31.98 Å
Total atoms total_atoms	5565
Residues n_residues	668
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	98.0 Å
Rg (real space) rg_real	31.97 Å
Rg uncertainty (real space) rg_real_error	0.64 Å
I(0) (real space) i0_real	9.4440e+07
I(0) uncertainty (real space) i0_real_error	1.3780e+06
Rg (reciprocal space) rg_reciprocal	32.03 Å
I(0) (reciprocal space) i0_reciprocal	94450000.0000
Solution quality estimate total_estimate	0.9128
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	40.0 Å
Skewness Skewness skewness	0.171
Kurtosis Kurtosis kurtosis	-0.570
Angular range angular_range	— – 0.2450 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	8527000.0000
Real-space data points n_real_points	50
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.975; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.938

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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	Radixin
Molecular weight formula_weight	37955.7 kDa
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	5565

GSMPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQARVDSSGRIVTD

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	house mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	P-selectin glycoprotein ligand 1
Molecular weight formula_weight	2240.6 kDa
Source method src_method	syn
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D,E

RLSRKTHMYPVRNYSPTE

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7. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d2emta1
Class class	a — All alpha proteins
Fold Fold fold	a.11 — Acyl-CoA binding protein-like
Superfamily Superfamily superfamily	a.11.2 — Second domain of FERM
Family Family family	a.11.2.1 — Second domain of FERM

Domain ID domain_id	d2emta2
Class class	b — All beta proteins
Fold Fold fold	b.55 — PH domain-like barrel
Superfamily Superfamily superfamily	b.55.1 — PH domain-like
Family Family family	b.55.1.5 — Third domain of FERM

Domain ID domain_id	d2emta3
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamily	d.15.1 — Ubiquitin-like
Family Family family	d.15.1.4 — First domain of FERM

Domain ID domain_id	d2emta4
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

Domain ID domain_id	d2emtb1
Class class	a — All alpha proteins
Fold Fold fold	a.11 — Acyl-CoA binding protein-like
Superfamily Superfamily superfamily	a.11.2 — Second domain of FERM
Family Family family	a.11.2.1 — Second domain of FERM

Domain ID domain_id	d2emtb2
Class class	b — All beta proteins
Fold Fold fold	b.55 — PH domain-like barrel
Superfamily Superfamily superfamily	b.55.1 — PH domain-like
Family Family family	b.55.1.5 — Third domain of FERM

Domain ID domain_id	d2emtb3
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamily	d.15.1 — Ubiquitin-like
Family Family family	d.15.1.4 — First domain of FERM

Domain ID domain_id	d2emtb4
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 (6 domains)

Domain ID domain_id	2emtA01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Domain ID domain_id	2emtA02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	80 — Acyl-CoA Binding Protein
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	2emtA03
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	29 — PH-domain like
Homologous superfamily homologous superfamily	30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Domain ID domain_id	2emtB01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Domain ID domain_id	2emtB02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	80 — Acyl-CoA Binding Protein
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	2emtB03
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	29 — PH-domain like
Homologous superfamily homologous superfamily	30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

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8. Citations (2)

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Unit-cell length a length_a	80.740 Å
Unit-cell length b length_b	85.730 Å
Unit-cell length c length_c	117.751 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	12

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	48.530 Å
R factor r_factor	0.2350
R_work r_work	0.2350
R_free r_free	0.2940

fit	/app/data/saxs_computation/em/2emt/2emt.fit
pddf	/app/data/pr_computation/em/2emt/2emt.pr.out
profile	/app/data/saxs_computation/em/2emt/2emt.dat

Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule PSGL-1

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

Radixin

State in the Current Structure

Other States of the Same Protein in the Database

P-selectin glycoprotein ligand 1

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (8 domains)

CATH v4.4 (6 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)