2lcr

NMR Structure of Alk1 extracellular domain

Method: SOLUTION NMR Dmax: 48.2 Å Quality: GOOD

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

Activin receptor-like kinase 1

Homo sapiens

UniProt P37023

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 22–118 Fragment:Extracellular domain residues 22-118 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 5.5;305 K;Pressure ambient NMR sample composition:0.5 mM [U-100% 15N] Alk1, 25 mM sodium phosphate, 0.02 % sodium azide, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.5 mM [U-100% 13C; U-100% 15N] Alk1, 25 mM sodium phosphate, 0.02 % sodium azide, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.5 mM [U-100% 13C; U-100% 15N] Alk1, 25 mM sodium phosphate, 0.02 % sodium azide, 5mg/mL mg Pf1 phage, 95% H2O/5% D2O | 95% H2O/5% 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.

6 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACVL1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–101; UniProt 22–118

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

SAXS profile for 2lcr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2lcr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2lcr
Deposition date deposition_date2011-05-06
Structure title titleNMR Structure of Alk1 extracellular domain
Keywords keywordsTRANSFERASE; TRANSFERASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.26
Radius of gyration Rg (electron density) rg_electron13.38
Forward intensity I(0) i0464275000.00
Molecular weight molecular_weight160700.0 kDa
Excluded volume excluded_volume192710 ų
Envelope volume envelope_volume28411 ų
Hydration-shell volume shell_volume14957 ų
Envelope diameter envelope_diameter56.1
Shell Rg shell_rg21.90
Envelope Rg envelope_rg16.50
Shape Rg shape_rg13.40
Total Rg total_rg13.52
Total atoms total_atoms21675
Residues n_residues1455
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax48.2
Rg (real space) rg_real13.26
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real4.6430e+08
I(0) uncertainty (real space) i0_real_error4.6970e+06
Rg (reciprocal space) rg_reciprocal13.26
I(0) (reciprocal space) i0_reciprocal464300000.0000
Solution quality estimate total_estimate0.7599
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary15.9
Skewness Skewness skewness0.391
Kurtosis Kurtosis kurtosis-0.041
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha388300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.666; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.878; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2lcrA00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59

8. Citations (1)

9. Files and Curves (10)