2d11

Crystal structure of the Radixin FERM domain complexed with the NHERF-2 C-terminal tail peptide

Method: X-RAY DIFFRACTION D_max: 158.0 Å Quality: GOOD

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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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–310	Fragment：FERM domain (residues 1-310)	Na(+)/H(+) exchange regulatory cofactor NHE-RF2 × 1 （Q15599）	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
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 1–310	Fragment：FERM domain (residues 1-310)	Na(+)/H(+) exchange regulatory cofactor NHE-RF2 × 1 （Q15599）	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
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 1–310	Fragment：FERM domain (residues 1-310)	Na(+)/H(+) exchange regulatory cofactor NHE-RF2 × 1 （Q15599）	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
4	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 1–310	Fragment：FERM domain (residues 1-310)	Na(+)/H(+) exchange regulatory cofactor NHE-RF2 × 1 （Q15599）	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

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 2D11	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 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 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 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 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
2D2Q Crystal structure of the dimerized radixin FERM domain Deposited 2005-09-15	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 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 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 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
2EMT Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule PSGL-1 Deposited 2007-03-28	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	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 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
2EMT Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule PSGL-1 Deposited 2007-03-28	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：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 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
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 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 17 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 Author chain C； PDBConstruct 3–312； UniProt 1–310 Author chain D； PDBConstruct 3–312； UniProt 1–310

Na(+)/H(+) exchange regulatory cofactor NHE-RF2

OrganismNot specified

UniProt Q15599

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain E； UniProt 310–337	Fragment：residues 310-337	Radixin × 1 （P26043）	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
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain F； UniProt 310–337	Fragment：residues 310-337	Radixin × 1 （P26043）	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
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain G； UniProt 310–337	Fragment：residues 310-337	Radixin × 1 （P26043）	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
4	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain H； UniProt 310–337	Fragment：residues 310-337	Radixin × 1 （P26043）	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

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 2D11	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2HE4 The crystal structure of the second PDZ domain of human NHERF-2 (SLC9A3R2) interacting with a mode 1 PDZ binding motif Deposited 2006-06-21	Different construct Different mutation/modification 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 147–232（86 aa） Fragment：PDZ 2 Domain (Residues 147-230)	Mutation：D229G	EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.45 Å R-free 0.180
2OCS The crystal structure of the first PDZ domain of human NHERF-2 (SLC9A3R2) Deposited 2006-12-21	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 9–91（83 aa）	Not recorded	SCN THIOCYANATE ION × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；298 K；20% PEG 3350, 0.20M KSCN, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 1.50 Å R-free 0.198
4P0C Crystal Structure of NHERF2 PDZ1 Domain in Complex with LPA2 Deposited 2014-02-20	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 9–90（82 aa） Fragment：UNP Q15599 residues 9-90; UNP Q9HBW0 residues 347-351	Not recorded	SCN THIOCYANATE ION × 1 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；100 mM sodium acetate, 0.2 M ammonium acetate	Resolution 1.34 Å R-free 0.177

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	NHRF2_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E； PDBConstruct 1–28； UniProt 310–337 Author chain F； PDBConstruct 1–28； UniProt 310–337 Author chain G； PDBConstruct 1–28； UniProt 310–337 Author chain H； PDBConstruct 1–28； UniProt 310–337

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.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2d11
Deposition date deposition_date	2005-08-11
Structure title title	Crystal structure of the Radixin FERM domain complexed with the NHERF-2 C-terminal tail peptide
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	42.74 Å
Radius of gyration Rg (electron density) rg_electron	43.07 Å
Forward intensity I(0) i0	309023000.00
Molecular weight molecular_weight	147720.0 kDa
Excluded volume excluded_volume	186740 Å³
Envelope volume envelope_volume	255690 Å³
Hydration-shell volume shell_volume	54044 Å³
Envelope diameter envelope_diameter	167.8 Å
Shell Rg shell_rg	43.67 Å
Envelope Rg envelope_rg	42.45 Å
Shape Rg shape_rg	43.06 Å
Total Rg total_rg	43.11 Å
Total atoms total_atoms	10438
Residues n_residues	1246
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	158.0 Å
Rg (real space) rg_real	43.18 Å
Rg uncertainty (real space) rg_real_error	2.18 Å
I(0) (real space) i0_real	3.0900e+08
I(0) uncertainty (real space) i0_real_error	6.6960e+06
Rg (reciprocal space) rg_reciprocal	42.75 Å
I(0) (reciprocal space) i0_reciprocal	308900000.0000
Solution quality estimate total_estimate	0.8055
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	42.7 Å
Skewness Skewness skewness	0.669
Kurtosis Kurtosis kurtosis	0.120
Angular range angular_range	— – 0.1850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	32380000.0000
Real-space data points n_real_points	38
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.595; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.829; Smooth: 0.854

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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	Radixin
Molecular weight formula_weight	36924.6 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	10601

GSMPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAR

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

Entity 2 Entity 2 polymer

Description description	Na(+)/H(+) exchange regulatory cofactor NHE-RF2
Molecular weight formula_weight	3517.1 kDa
Source method src_method	syn
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,F,G,H

KEKARAMRVNKRAPQMDWNRKREIFSNF

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	163

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7. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (12 domains)

Domain ID domain_id	d2d11a1
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	d2d11a2
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	d2d11a3
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	d2d11b1
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	d2d11b2
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	d2d11b3
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	d2d11c1
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	d2d11c2
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	d2d11c3
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	d2d11d1
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	d2d11d2
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	d2d11d3
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

CATH v4.4 (12 domains)

Domain ID domain_id	2d11A01
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	2d11A02
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	2d11A03
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	2d11B01
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	2d11B02
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	2d11B03
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	2d11C01
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	2d11C02
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	2d11C03
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	2d11D01
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	2d11D02
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	2d11D03
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)

▶

8. Citations (4)

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Unit-cell length a length_a	68.626 Å
Unit-cell length b length_b	144.375 Å
Unit-cell length c length_c	177.944 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	16

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

Resolution resolution	2.810 Å
Low-resolution limit resolution_low	29.700 Å
R factor r_factor	0.2234
R_work r_work	0.2219
R_free r_free	0.2782

fit	/app/data/saxs_computation/d1/2d11/2d11.fit
pddf	/app/data/pr_computation/d1/2d11/2d11.pr.out
profile	/app/data/saxs_computation/d1/2d11/2d11.dat

Crystal structure of the Radixin FERM domain complexed with the NHERF-2 C-terminal tail peptide

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

Na(+)/H(+) exchange regulatory cofactor NHE-RF2

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

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (12 domains)

CATH v4.4 (12 domains)

8. Citations (4)

9. Files and Curves (10)

Files (7)

Curves (3)