7mgc

Concanavalin A bound to a DNA glycoconjugate, G(Man-T)AC

Method: X-RAY DIFFRACTION Dmax: 91.0 Å Quality: EXCELLENT

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

Concanavalin-A

OrganismNot specified

UniProt P02866

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 164–281 Chain A; UniProt 30–148 Chain B; UniProt 164–281 Chain B; UniProt 30–148 Chain C; UniProt 164–281 Chain C; UniProt 30–148 Chain D; UniProt 164–281 Chain D; UniProt 30–148 Not recorded MMA methyl alpha-D-mannopyranoside × 4 MN MANGANESE (II) ION × 4 CA CALCIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;295 K;Sitting drop comprising 1 uL of Concanavalin A (40 uM) and G(Man-T)AC (160 uM) + 1 uL crystallization condition (Helix screen, condition H6: 0.1 M potassium chloride, 0.002 M spermine tetrahydrochloride, 0.05 M bis-Tris (pH 7), 15% w/v PEG 2000 MME). Reservoir contained 70 uL of crystallization condition Resolution 2.92 Å R-free 0.277

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.

72 other PDB entries and 89 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CONA_CANEN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–118; UniProt 164–281 Author chain A; PDBConstruct 119–237; UniProt 30–148 Author chain B; PDBConstruct 1–118; UniProt 164–281 Author chain B; PDBConstruct 119–237; UniProt 30–148 Author chain C; PDBConstruct 1–118; UniProt 164–281 Author chain C; PDBConstruct 119–237; UniProt 30–148 Author chain D; PDBConstruct 1–118; UniProt 164–281 Author chain D; PDBConstruct 119–237; UniProt 30–148

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 7mgc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7mgc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7mgc
Deposition date deposition_date2021-04-12
Structure title titleConcanavalin A bound to a DNA glycoconjugate, G(Man-T)AC
Keywords keywordsLectin, DNA complex, SUGAR BINDING PROTEIN, SUGAR BINDING PROTEIN-DNA complex; SUGAR BINDING PROTEIN/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.87
Radius of gyration Rg (electron density) rg_electron29.53
Forward intensity I(0) i0158116000.00
Molecular weight molecular_weight98033.0 kDa
Excluded volume excluded_volume121630 ų
Envelope volume envelope_volume151530 ų
Hydration-shell volume shell_volume42061 ų
Envelope diameter envelope_diameter94.9
Shell Rg shell_rg37.21
Envelope Rg envelope_rg29.22
Shape Rg shape_rg29.53
Total Rg total_rg30.22
Total atoms total_atoms6919
Residues n_residues934
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 dmax91.0
Rg (real space) rg_real30.64
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real1.5810e+08
I(0) uncertainty (real space) i0_real_error2.1580e+06
Rg (reciprocal space) rg_reciprocal30.74
I(0) (reciprocal space) i0_reciprocal158100000.0000
Solution quality estimate total_estimate0.9093
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.8
Skewness Skewness skewness0.004
Kurtosis Kurtosis kurtosis-0.677
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha39730000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.966; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.931

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd7mgca_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.1 — Legume lectins
Domain ID domain_idd7mgcb_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.1 — Legume lectins
Domain ID domain_idd7mgcc_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.1 — Legume lectins
Domain ID domain_idd7mgcd_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.1 — Legume lectins

8. Citations (1)

9. Files and Curves (10)