1mwp

N-TERMINAL DOMAIN OF THE AMYLOID PRECURSOR PROTEIN

Method: X-RAY DIFFRACTION Dmax: 52.0 Å Quality: GOOD

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

AMYLOID A4 PROTEIN

Homo sapiens

UniProt P05067

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 28–123 Fragment:HEPARIN BINDING DOMAIN No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;pH 7.5 Resolution 1.80 Å R-free 0.242

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.

211 other PDB entries and 282 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–96; UniProt 28–123

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 1mwp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1mwp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1mwp
Deposition date deposition_date1999-03-09
Structure title titleN-TERMINAL DOMAIN OF THE AMYLOID PRECURSOR PROTEIN
Keywords keywordsHEPARIN BINDING, SUGAR BINDING PROTEIN; SUGAR BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier14.14
Radius of gyration Rg (electron density) rg_electron13.16
Forward intensity I(0) i02662210.00
Molecular weight molecular_weight11040.0 kDa
Excluded volume excluded_volume13722 ų
Envelope volume envelope_volume15384 ų
Hydration-shell volume shell_volume10225 ų
Envelope diameter envelope_diameter50.8
Shell Rg shell_rg18.46
Envelope Rg envelope_rg13.77
Shape Rg shape_rg13.15
Total Rg total_rg14.39
Total atoms total_atoms771
Residues n_residues96
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 dmax52.0
Rg (real space) rg_real14.11
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real2.6620e+06
I(0) uncertainty (real space) i0_real_error2.7820e+04
Rg (reciprocal space) rg_reciprocal14.11
I(0) (reciprocal space) i0_reciprocal2662000.0000
Solution quality estimate total_estimate0.8252
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.1
Skewness Skewness skewness0.365
Kurtosis Kurtosis kurtosis0.095
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha544900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.601; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.931; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1mwpa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.170 — SRCR-like
Superfamily Superfamily superfamilyd.170.2 — A heparin-binding domain
Family Family familyd.170.2.1 — A heparin-binding domain

CATH v4.4 (1 domains)

Domain ID domain_id1mwpA00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology570 — Sugar Binding Protein, Amyloid A4 Protein; Chain A
Homologous superfamily homologous superfamily10 — Amyloidogenic glycoprotein, heparin-binding domain

8. Citations (1)

9. Files and Curves (10)