1e6f

Human MIR-receptor, repeat 11

Method: X-RAY DIFFRACTION Dmax: 72.8 Å Quality: GOOD

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

CATION-INDEPENDENT MANNOSE-6-PHOSPHATE RECEPTOR

HOMO SAPIENS

UniProt P11717

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 1508–1650 Fragment:IGF-II-BINDING DOMAIN, REPEAT 11, RESIDUES 1508-1650 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;PRECIPITANT: 0.2 M AMMONIUM ACETATE, 0.1 M CACODYLATE PH 5 28% PEG 4000. PROTEIN SOLUTION: 8 MG/ML IN 10 MM TRIS-HCL PH7.5, 150 MM N VAPOUR DIFFUSION, HANGING DROPS,1:1 RATIO. Resolution 1.75 Å R-free 0.273
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1508–1650 Fragment:IGF-II-BINDING DOMAIN, REPEAT 11, RESIDUES 1508-1650 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;PRECIPITANT: 0.2 M AMMONIUM ACETATE, 0.1 M CACODYLATE PH 5 28% PEG 4000. PROTEIN SOLUTION: 8 MG/ML IN 10 MM TRIS-HCL PH7.5, 150 MM N VAPOUR DIFFUSION, HANGING DROPS,1:1 RATIO. Resolution 1.75 Å R-free 0.273

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.

19 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MPRI_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–143; UniProt 1508–1650 Author chain B; PDBConstruct 1–143; UniProt 1508–1650

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 1e6f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1e6f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1e6f
Deposition date deposition_date2000-08-15
Structure title titleHuman MIR-receptor, repeat 11
Keywords keywordsRECEPTOR, MIR-RECEPTOR, IGF-II RECEPTOR, TRANSPORT, GLYCOPROTEIN; RECEPTOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.11
Radius of gyration Rg (electron density) rg_electron20.44
Forward intensity I(0) i014252400.00
Molecular weight molecular_weight27871.0 kDa
Excluded volume excluded_volume34699 ų
Envelope volume envelope_volume41318 ų
Hydration-shell volume shell_volume17447 ų
Envelope diameter envelope_diameter73.6
Shell Rg shell_rg26.27
Envelope Rg envelope_rg20.80
Shape Rg shape_rg20.42
Total Rg total_rg21.35
Total atoms total_atoms1949
Residues n_residues260
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 dmax72.8
Rg (real space) rg_real21.13
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real1.4250e+07
I(0) uncertainty (real space) i0_real_error2.0400e+05
Rg (reciprocal space) rg_reciprocal21.13
I(0) (reciprocal space) i0_reciprocal14250000.0000
Solution quality estimate total_estimate0.8746
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.5
Skewness Skewness skewness0.349
Kurtosis Kurtosis kurtosis-0.330
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1889000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.831; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.921; Smooth: 0.952

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1e6fa_
Class classb — All beta proteins
Fold Fold foldb.64 — Mannose 6-phosphate receptor domain
Superfamily Superfamily superfamilyb.64.1 — Mannose 6-phosphate receptor domain
Family Family familyb.64.1.1 — Mannose 6-phosphate receptor domain
Domain ID domain_idd1e6fb_
Class classb — All beta proteins
Fold Fold foldb.64 — Mannose 6-phosphate receptor domain
Superfamily Superfamily superfamilyb.64.1 — Mannose 6-phosphate receptor domain
Family Family familyb.64.1.1 — Mannose 6-phosphate receptor domain

CATH v4.4 (2 domains)

Domain ID domain_id1e6fA00
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology130 — Cation-dependent Mannose-6-phosphate Receptor; Chain A
Homologous superfamily homologous superfamily10 — Mannose-6-phosphate receptor binding domain
Domain ID domain_id1e6fB00
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology130 — Cation-dependent Mannose-6-phosphate Receptor; Chain A
Homologous superfamily homologous superfamily10 — Mannose-6-phosphate receptor binding domain

8. Citations (1)

9. Files and Curves (10)