1rdl

MANNOSE-BINDING PROTEIN, SUBTILISIN DIGEST FRAGMENT COMPLEX WITH ALPHA-METHYL-D-MANNOPYRANOSIDE (0.2 M)

Method: X-RAY DIFFRACTION Dmax: 69.1 Å Quality: GOOD

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

MANNOSE-BINDING PROTEIN-C

Rattus rattus

UniProt P08661

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain 1; UniProt 132–244 Chain 2; UniProt 132–244 Fragment:SUBTILISIN FRAGMENT (RESIDUES 114 - 226) MMA methyl alpha-D-mannopyranoside × 2 CA CALCIUM ION × 4 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.4;pH 7.4 Resolution 1.70 Å R-free 0.230

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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MBL2_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain 1; PDBConstruct 1–113; UniProt 132–244 Author chain 2; PDBConstruct 1–113; UniProt 132–244

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 1rdl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1rdl
Deposition date deposition_date1995-09-05
Structure title titleMANNOSE-BINDING PROTEIN, SUBTILISIN DIGEST FRAGMENT COMPLEX WITH ALPHA-METHYL-D-MANNOPYRANOSIDE (0.2 M)
Keywords keywordsC-TYPE LECTIN, CALCIUM-BINDING PROTEIN, LECTIN; LECTIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.53
Radius of gyration Rg (electron density) rg_electron20.71
Forward intensity I(0) i012871700.00
Molecular weight molecular_weight25498.0 kDa
Excluded volume excluded_volume31270 ų
Envelope volume envelope_volume36981 ų
Hydration-shell volume shell_volume16156 ų
Envelope diameter envelope_diameter71.1
Shell Rg shell_rg25.16
Envelope Rg envelope_rg20.79
Shape Rg shape_rg20.73
Total Rg total_rg21.27
Total atoms total_atoms1777
Residues n_residues223
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 dmax69.1
Rg (real space) rg_real21.71
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real1.2870e+07
I(0) uncertainty (real space) i0_real_error1.7300e+05
Rg (reciprocal space) rg_reciprocal21.68
I(0) (reciprocal space) i0_reciprocal12870000.0000
Solution quality estimate total_estimate0.7739
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.3
Skewness Skewness skewness0.475
Kurtosis Kurtosis kurtosis-0.518
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3171000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.745; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.829; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1rdl1_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.169 — C-type lectin-like
Superfamily Superfamily superfamilyd.169.1 — C-type lectin-like
Family Family familyd.169.1.1 — C-type lectin domain
Domain ID domain_idd1rdl2_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.169 — C-type lectin-like
Superfamily Superfamily superfamilyd.169.1 — C-type lectin-like
Family Family familyd.169.1.1 — C-type lectin domain

CATH v4.4 (2 domains)

Domain ID domain_id1rdl100
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology100 — Mannose-Binding Protein A; Chain A
Homologous superfamily homologous superfamily10 — Mannose-Binding Protein A, subunit A
Domain ID domain_id1rdl200
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology100 — Mannose-Binding Protein A; Chain A
Homologous superfamily homologous superfamily10 — Mannose-Binding Protein A, subunit A

8. Citations (5)

9. Files and Curves (10)