1kze

Complex of MBP-C and bivalent Man-terminated glycopeptide

Method: X-RAY DIFFRACTION Dmax: 71.1 Å Quality: GOOD

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

MANNOSE-BINDING PROTEIN C

Rattus norvegicus

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 129–243 Chain 2; UniProt 129–243 Fragment:SUBTILISIN FRAGMENT (RESIDUES 129-243 of P08661) MAN alpha-D-mannopyranose × 2 CA CALCIUM ION × 4 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;298 K;PEG 8000, Tris-Cl, NaCl, CaCl2, NaN3, pH 7.4, VAPOR DIFFUSION, HANGING DROP at 298K Resolution 1.80 Å R-free 0.243

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 1–115; UniProt 129–243 Author chain 2; PDBConstruct 1–115; UniProt 129–243

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 1kze

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1kze
Deposition date deposition_date2002-02-06
Structure title titleComplex of MBP-C and bivalent Man-terminated glycopeptide
Keywords keywordsprotein-carbohydrate complex, IMMUNE SYSTEM, SUGAR BINDING PROTEIN; IMMUNE SYSTEM, SUGAR BINDING PROTEIN
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_electron20.69
Forward intensity I(0) i012981500.00
Molecular weight molecular_weight25519.0 kDa
Excluded volume excluded_volume31276 ų
Envelope volume envelope_volume36966 ų
Hydration-shell volume shell_volume16172 ų
Envelope diameter envelope_diameter71.6
Shell Rg shell_rg25.15
Envelope Rg envelope_rg20.75
Shape Rg shape_rg20.70
Total Rg total_rg21.25
Total atoms total_atoms1778
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 dmax71.1
Rg (real space) rg_real21.70
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real1.2980e+07
I(0) uncertainty (real space) i0_real_error1.7050e+05
Rg (reciprocal space) rg_reciprocal21.67
I(0) (reciprocal space) i0_reciprocal12980000.0000
Solution quality estimate total_estimate0.8437
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.9
Skewness Skewness skewness0.477
Kurtosis Kurtosis kurtosis-0.512
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3383000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.728; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.794; Smooth: 0.986

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_idd1kze1_
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_idd1kze2_
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_id1kze100
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_id1kze200
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)