1rir

Crystal structure of meso-tetrasulphonatophenylporphyrin in complex with Peanut lectin.

Method: X-RAY DIFFRACTION Dmax: 112.5 Å Quality: GOOD

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

Galactose-binding lectin

OrganismNot specified

UniProt P02872

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 24–259 Chain B; UniProt 24–259 Chain C; UniProt 24–259 Chain D; UniProt 24–259 Not recorded CA CALCIUM ION × 4 MN MANGANESE (II) ION × 4 SFP 5,10,15,20-TETRAKIS(4-SULPFONATOPHENYL)-21H,23H-PORPHINE × 11 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;298 K;ammonium sulphate, Sodium Chloride, Phosphate buffer, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 2.90 Å R-free 0.282

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.

25 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LECG_ARAHY
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–236; UniProt 24–259 Author chain B; PDBConstruct 1–236; UniProt 24–259 Author chain C; PDBConstruct 1–236; UniProt 24–259 Author chain D; PDBConstruct 1–236; UniProt 24–259

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 1rir

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1rir
Deposition date deposition_date2003-11-17
Structure title titleCrystal structure of meso-tetrasulphonatophenylporphyrin in complex with Peanut lectin.
Keywords keywordsSUGAR 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_guinier32.42
Radius of gyration Rg (electron density) rg_electron31.14
Forward intensity I(0) i0189825000.00
Molecular weight molecular_weight109360.0 kDa
Excluded volume excluded_volume135920 ų
Envelope volume envelope_volume170550 ų
Hydration-shell volume shell_volume44530 ų
Envelope diameter envelope_diameter117.0
Shell Rg shell_rg39.02
Envelope Rg envelope_rg31.44
Shape Rg shape_rg31.09
Total Rg total_rg31.90
Total atoms total_atoms7684
Residues n_residues928
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 dmax112.5
Rg (real space) rg_real32.26
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real1.8980e+08
I(0) uncertainty (real space) i0_real_error3.0780e+06
Rg (reciprocal space) rg_reciprocal32.33
I(0) (reciprocal space) i0_reciprocal189800000.0000
Solution quality estimate total_estimate0.8720
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary43.6
Skewness Skewness skewness0.183
Kurtosis Kurtosis kurtosis-0.396
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha36710000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.778; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1rira_
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_idd1rirb_
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_idd1rirc_
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_idd1rird_
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

CATH v4.4 (4 domains)

Domain ID domain_id1rirA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200
Domain ID domain_id1rirB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200
Domain ID domain_id1rirC00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200
Domain ID domain_id1rirD00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200

8. Citations (2)

9. Files and Curves (10)