SAXSdb — 2ltn

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

PEA LECTIN, ALPHA CHAIN

Pisum sativum

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 31–211 Chain B； UniProt 218–269 Chain C； UniProt 31–211 Chain D； UniProt 218–269	Not recorded	MN MANGANESE (II) ION × 2 CA CALCIUM ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 1.70 Å
2	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 31–211 Chain D； UniProt 218–269	Not recorded	MN MANGANESE (II) ION × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 1.70 Å
3	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 31–211 Chain B； UniProt 218–269	Not recorded	MN MANGANESE (II) ION × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 1.70 Å

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.

Other PDB	Difference from Current Entry 2LTN	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BQP THE STRUCTURE OF THE PEA LECTIN-D-MANNOPYRANOSE COMPLEX Deposited 1998-08-17	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 31–211（181 aa） Fragment：BETA CHAIN Chain B 218–264（47 aa） Fragment：ALPHA CHAIN	Not recorded	CA CALCIUM ION × 1 MN MANGANESE (II) ION × 1 MAN alpha-D-mannopyranose × 1 BMA beta-D-mannopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；pH 7.0	Resolution 2.10 Å R-free 0.188
1BQP THE STRUCTURE OF THE PEA LECTIN-D-MANNOPYRANOSE COMPLEX Deposited 1998-08-17	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 31–211（181 aa） Fragment：BETA CHAIN Chain D 218–264（47 aa） Fragment：ALPHA CHAIN	Not recorded	CA CALCIUM ION × 1 MN MANGANESE (II) ION × 1 MAN alpha-D-mannopyranose × 1 BMA beta-D-mannopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；pH 7.0	Resolution 2.10 Å R-free 0.188
1BQP THE STRUCTURE OF THE PEA LECTIN-D-MANNOPYRANOSE COMPLEX Deposited 1998-08-17	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 31–211（181 aa） Fragment：BETA CHAIN Chain B 218–264（47 aa） Fragment：ALPHA CHAIN Chain C 31–211（181 aa） Fragment：BETA CHAIN Chain D 218–264（47 aa） Fragment：ALPHA CHAIN	Not recorded	CA CALCIUM ION × 2 MN MANGANESE (II) ION × 2 MAN alpha-D-mannopyranose × 2 BMA beta-D-mannopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；pH 7.0	Resolution 2.10 Å R-free 0.188
1HKD Structure of pea lectin in complex with alpha-methyl-D-glucopyranoside Deposited 2003-03-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 31–211（181 aa） Fragment：RESIDUES 31-211 Chain B 218–269（52 aa） Fragment：RESIDUES 218-269 Chain C 31–211（181 aa） Fragment：RESIDUES 31-211 Chain D 218–269（52 aa） Fragment：RESIDUES 218-269	Not recorded	CA CALCIUM ION × 2 MN MANGANESE (II) ION × 2 GYP methyl alpha-D-glucopyranoside × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；1.7 M AMMONIUM SULFATE, 10% (V/V) ETHANOL, pH 7.00	Resolution 2.09 Å R-free 0.209
1OFS Pea lectin-sucrose complex Deposited 2003-04-19	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 31–217（187 aa） Fragment：RESIDUES 31-217 Chain B 218–265（48 aa） Fragment：RESIDUES 218-265 Chain C 31–217（187 aa） Fragment：RESIDUES 31-217 Chain D 218–265（48 aa） Fragment：RESIDUES 218-265	Not recorded	MN MANGANESE (II) ION × 2 CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；0.1 M MES PH 6.5, 12% (W/V) PEG 20K, 8% (V/V) ETOH, 40 MM SUCROSE; CRYOSOLUTION: 0.1 M MES PH 6.5, 17% PEG 20K, 60% (V/V) ETOH, 25 MM SUCROSE	Resolution 1.80 Å R-free 0.207
1RIN X-RAY CRYSTAL STRUCTURE OF A PEA LECTIN-TRIMANNOSIDE COMPLEX AT 2.6 ANGSTROMS RESOLUTION Deposited 1993-01-27	Different construct Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 31–210（180 aa） Chain B 218–266（49 aa） Chain C 31–210（180 aa） Chain D 218–266（49 aa）	Not recorded	MAN alpha-D-mannopyranose × 2 MN MANGANESE (II) ION × 2 CA CALCIUM ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.60 Å
1RIN X-RAY CRYSTAL STRUCTURE OF A PEA LECTIN-TRIMANNOSIDE COMPLEX AT 2.6 ANGSTROMS RESOLUTION Deposited 1993-01-27	Different construct Different ligand/ion Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 31–210（180 aa） Chain B 218–266（49 aa）	Not recorded	MAN alpha-D-mannopyranose × 1 MN MANGANESE (II) ION × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.60 Å
1RIN X-RAY CRYSTAL STRUCTURE OF A PEA LECTIN-TRIMANNOSIDE COMPLEX AT 2.6 ANGSTROMS RESOLUTION Deposited 1993-01-27	Different construct Different ligand/ion Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 31–210（180 aa） Chain D 218–266（49 aa）	Not recorded	MAN alpha-D-mannopyranose × 1 MN MANGANESE (II) ION × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.60 Å
2BQP THE STRUCTURE OF THE PEA LECTIN-D-GLUCOPYRANOSE COMPLEX Deposited 1998-12-08	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 31–264（234 aa） Chain B 31–264（234 aa）	Not recorded	GLC alpha-D-glucopyranose × 2 CA CALCIUM ION × 2 MN MANGANESE (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；pH 7.0	Resolution 1.90 Å R-free 0.188
5T7P Crystal structure of Pisum arvense lectin (PAL) complexed with X-Man Deposited 2016-09-05	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 31–266（236 aa） Fragment：UNP residues 31-266 Chain B 31–266（236 aa） Fragment：UNP residues 31-266	Not recorded	MN MANGANESE (II) ION × 2 CA CALCIUM ION × 2 XMM 5-bromo-4-chloro-1H-indol-3-yl alpha-D-mannopyranoside × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；100 mM HEPES pH 6.8, 20% PEG 8000, 200 mM Magnesium acetate tetrahydrate	Resolution 2.16 Å R-free 0.221

6 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	LEC_PEA
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 1–181； UniProt 31–211 Author chain C； PDBConstruct 1–181； UniProt 31–211 Author chain B； PDBConstruct 1–52； UniProt 218–269 Author chain D； PDBConstruct 1–52； UniProt 218–269

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2ltn
Deposition date deposition_date	1990-06-26
Structure title title	DESIGN, EXPRESSION, AND CRYSTALLIZATION OF RECOMBINANT LECTIN FROM THE GARDEN PEA (PISUM SATIVUM)
Keywords keywords	LECTIN; LECTIN
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	25.82 Å
Radius of gyration Rg (electron density) rg_electron	24.83 Å
Forward intensity I(0) i0	41359900.00
Molecular weight molecular_weight	50488.0 kDa
Excluded volume excluded_volume	63284 Å³
Envelope volume envelope_volume	72612 Å³
Hydration-shell volume shell_volume	25167 Å³
Envelope diameter envelope_diameter	90.5 Å
Shell Rg shell_rg	31.32 Å
Envelope Rg envelope_rg	25.04 Å
Shape Rg shape_rg	24.80 Å
Total Rg total_rg	25.67 Å
Total atoms total_atoms	3572
Residues n_residues	458
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	86.5 Å
Rg (real space) rg_real	25.93 Å
Rg uncertainty (real space) rg_real_error	0.62 Å
I(0) (real space) i0_real	4.1360e+07
I(0) uncertainty (real space) i0_real_error	6.1970e+05
Rg (reciprocal space) rg_reciprocal	25.90 Å
I(0) (reciprocal space) i0_reciprocal	41360000.0000
Solution quality estimate total_estimate	0.8705
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	25.5 Å
Skewness Skewness skewness	0.470
Kurtosis Kurtosis kurtosis	-0.355
Angular range angular_range	— – 0.3050 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	7213000.0000
Real-space data points n_real_points	62
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.806; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.913; Smooth: 0.982

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	PEA LECTIN, ALPHA CHAIN
Molecular weight formula_weight	20001.1 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C
Atom count atom_count	3866

TETTSFLITKFSPDQQNLIFQGDGYTTKEKLTLTKAVKNTVGRALYSSPIHIWDRETGNVANFVTSFTFVINAPNSYNVADGFTFFIAPVDTKPQTGGGYLGVFNSAEYDKTTQTVAVEFDTFYNAAWDPSNRDRHIGIDVNSIKSVNTKSWKLQNGEEANVVIAFNAATNVLTVSLTYPN

来源 Source

来源生物 organism	Pisum sativum
通用名 common_name	pea
NCBI Class编号 ncbi_taxonomy_id	3888
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	PEA LECTIN, BETA CHAIN
Molecular weight formula_weight	5596.1 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D

VTSYTLSDVVSLKDVVPEWVRIGFSATTGAEYAAHEVLSWSFHSELSGTSSS

来源 Source

来源生物 organism	Pisum sativum
通用名 common_name	pea
NCBI Class编号 ncbi_taxonomy_id	3888

Entity 3 Entity 3 non-polymer

Description description	MANGANESE (II) ION
Molecular weight formula_weight	54.9 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	294

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2ltn.1
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.1 — Legume lectins

Domain ID domain_id	d2ltn.2
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.1 — Legume lectins

CATH v4.4 (2 domains)

Domain ID domain_id	2ltnA00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	200 —

Domain ID domain_id	2ltnC00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	200 —

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8. Citations (4)

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Unit-cell length a length_a	50.730 Å
Unit-cell length b length_b	61.160 Å
Unit-cell length c length_c	136.590 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	1.700 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	0.1770
R_work r_work	—
R_free r_free	—

fit	/app/data/saxs_computation/lt/2ltn/2ltn.fit
pddf	/app/data/pr_computation/lt/2ltn/2ltn.pr.out
profile	/app/data/saxs_computation/lt/2ltn/2ltn.dat

DESIGN, EXPRESSION, AND CRYSTALLIZATION OF RECOMBINANT LECTIN FROM THE GARDEN PEA (PISUM SATIVUM)

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

PEA LECTIN, ALPHA CHAIN

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (4)

9. Files and Curves (10)

Files (7)

Curves (3)