2ric

Crystal structure of the trimeric neck and carbohydrate recognition domain of human surfactant protein D in complex with L-glycero-D-manno-heptopyranosyl-(1-3)-L-glycero-D-manno-heptopyranose

Method: X-RAY DIFFRACTION Dmax: 86.0 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 2 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 223–375 Chain B; UniProt 223–375 Chain C; UniProt 223–375 Fragment:neck and carbohydrate recognition domain L-glycero-alpha-D-manno-heptopyranose-(1-3)-L-glycero-alpha-D-manno-heptopyranose × 2 CA CALCIUM ION × 9 GMH L-glycero-alpha-D-manno-heptopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;290 K;12% PEG 8000, 150MM NACL, 10MM CACL2, 100MM HEPES , PH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 1.80 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.

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 8–160; UniProt 223–375 Author chain B; PDBConstruct 8–160; UniProt 223–375 Author chain C; PDBConstruct 8–160; UniProt 223–375

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 2ric

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ric
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2ric
Deposition date deposition_date2007-10-10
Structure title titleCrystal structure of the trimeric neck and carbohydrate recognition domain of human surfactant protein D in complex with L-glycero-D-manno-heptopyranosyl-(1-3)-L-glycero-D-manno-heptopyranose
Keywords keywordsSURFACTANT PROTEIN; CARBOHYDRATE RECOGNITION; DOMAIN TRIMERIC, 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_guinier27.51
Radius of gyration Rg (electron density) rg_electron26.27
Forward intensity I(0) i046649700.00
Molecular weight molecular_weight51670.0 kDa
Excluded volume excluded_volume64026 ų
Envelope volume envelope_volume77075 ų
Hydration-shell volume shell_volume25899 ų
Envelope diameter envelope_diameter93.7
Shell Rg shell_rg31.81
Envelope Rg envelope_rg26.47
Shape Rg shape_rg26.21
Total Rg total_rg27.05
Total atoms total_atoms3617
Residues n_residues465
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 dmax86.0
Rg (real space) rg_real27.40
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real4.6650e+07
I(0) uncertainty (real space) i0_real_error6.7570e+05
Rg (reciprocal space) rg_reciprocal27.44
I(0) (reciprocal space) i0_reciprocal46650000.0000
Solution quality estimate total_estimate0.9014
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.0
Skewness Skewness skewness0.070
Kurtosis Kurtosis kurtosis-0.711
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14130000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 11 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd2rica1
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.169.1.0 — automated matches
Domain ID domain_idd2rica2
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_idd2rica3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2ricb1
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.169.1.0 — automated matches
Domain ID domain_idd2ricb2
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_idd2ricc1
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.169.1.0 — automated matches
Domain ID domain_idd2ricc2
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_idd2ricc3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (3 domains)

Domain ID domain_id2ricA00
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_id2ricB00
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_id2ricC00
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 (1)

9. Files and Curves (10)