5oxs

Crystal structure of human lung surfactant protein D trimeric fragment with bound ligand Salmonella enterica Minnesota R5 oligosaccharide

Method: X-RAY DIFFRACTION Dmax: 82.0 Å Quality: EXCELLENT

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

Pulmonary surfactant-associated protein D

Homo sapiens

UniProt P35247

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Homooligomer Protein × 3 其他Polymer 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 201–375 Chain B; UniProt 201–375 Chain C; UniProt 201–375 Fragment:Trimeric neck + carbohydrate recognition domain ;alpha-D-glucopyranose-(1-3)-L-glycero-alpha-D-manno-heptopyranose-(1-3)-L-glycero-alpha-D-manno-heptopyranose-(1-5)-4,7-anhydro-3-deoxy-D-gluco-oct-2-ulosonic acid ; × 3 CA CALCIUM ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;0.1M Tris pH 8.0, 16% PEG 6000 Resolution 1.65 Å R-free 0.187

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.

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

View Construct and Data Evidence
UniProt name SFTPD_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–177; UniProt 201–375 Author chain B; PDBConstruct 3–177; UniProt 201–375 Author chain C; PDBConstruct 3–177; UniProt 201–375

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 5oxs

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5oxs
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5oxs
Deposition date deposition_date2017-09-07
Structure title titleCrystal structure of human lung surfactant protein D trimeric fragment with bound ligand Salmonella enterica Minnesota R5 oligosaccharide
Keywords keywords;trimeric recombinant collectin fragment, neck+CRD, alpha-helical coiled coil, carbohydrate recognition domain, lectin, sugar binding protein, SURFACTANT PROTEIN ;; SURFACTANT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.56
Radius of gyration Rg (electron density) rg_electron26.27
Forward intensity I(0) i047842100.00
Molecular weight molecular_weight52215.0 kDa
Excluded volume excluded_volume64705 ų
Envelope volume envelope_volume81272 ų
Hydration-shell volume shell_volume26847 ų
Envelope diameter envelope_diameter86.0
Shell Rg shell_rg32.32
Envelope Rg envelope_rg26.47
Shape Rg shape_rg26.22
Total Rg total_rg27.06
Total atoms total_atoms3660
Residues n_residues458
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 dmax82.0
Rg (real space) rg_real27.41
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real4.7840e+07
I(0) uncertainty (real space) i0_real_error5.8060e+05
Rg (reciprocal space) rg_reciprocal27.46
I(0) (reciprocal space) i0_reciprocal47840000.0000
Solution quality estimate total_estimate0.9108
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.0
Skewness Skewness skewness0.028
Kurtosis Kurtosis kurtosis-0.753
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15980000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.953; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd5oxsa1
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.1 — Triple coiled coil domain of C-type lectins
Family Family familyh.1.1.1 — Triple coiled coil domain of C-type lectins
Domain ID domain_idd5oxsa2
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_idd5oxsb1
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.1 — Triple coiled coil domain of C-type lectins
Family Family familyh.1.1.1 — Triple coiled coil domain of C-type lectins
Domain ID domain_idd5oxsb2
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_idd5oxsc1
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.1 — Triple coiled coil domain of C-type lectins
Family Family familyh.1.1.1 — Triple coiled coil domain of C-type lectins
Domain ID domain_idd5oxsc2
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 (3 domains)

Domain ID domain_id5oxsA00
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_id5oxsB00
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_id5oxsC00
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 (2)

9. Files and Curves (10)