SAXSdb — 1elp

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

GAMMA-D CRYSTALLIN

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CRGD_BOVIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–173； UniProt 1–173 Author chain B； PDBConstruct 1–173； UniProt 1–173

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	1elp
Deposition date deposition_date	1995-12-20
Structure title title	GAMMA-D CRYSTALLIN STRUCTURE AT 1.95 A RESOLUTION
Keywords keywords	EYE LENS PROTEIN; EYE LENS PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1elp__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1elp__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1elp__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	28.53 Å
Rg (electron density)	28.36 Å
Total Rg	28.77 Å
Atom count	2928
Residues	346
Excluded volume	50956 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1elp__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (2)

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1elpa1
Class class	b — All beta proteins
Fold Fold fold	b.11 — gamma-Crystallin-like
Superfamily Superfamily superfamily	b.11.1 — gamma-Crystallin-like
Family Family family	b.11.1.1 — Crystallins/Ca-binding development proteins

Domain ID domain_id	d1elpa2
Class class	b — All beta proteins
Fold Fold fold	b.11 — gamma-Crystallin-like
Superfamily Superfamily superfamily	b.11.1 — gamma-Crystallin-like
Family Family family	b.11.1.1 — Crystallins/Ca-binding development proteins

Domain ID domain_id	d1elpb1
Class class	b — All beta proteins
Fold Fold fold	b.11 — gamma-Crystallin-like
Superfamily Superfamily superfamily	b.11.1 — gamma-Crystallin-like
Family Family family	b.11.1.1 — Crystallins/Ca-binding development proteins

Domain ID domain_id	d1elpb2
Class class	b — All beta proteins
Fold Fold fold	b.11 — gamma-Crystallin-like
Superfamily Superfamily superfamily	b.11.1 — gamma-Crystallin-like
Family Family family	b.11.1.1 — Crystallins/Ca-binding development proteins

CATH v4.4 (4 domains)

Domain ID domain_id	1elpA01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	20 — Gamma-B Crystallin; domain 1
Homologous superfamily homologous superfamily	10 — Crystallins

Domain ID domain_id	1elpA02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	20 — Gamma-B Crystallin; domain 1
Homologous superfamily homologous superfamily	10 — Crystallins

Domain ID domain_id	1elpB01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	20 — Gamma-B Crystallin; domain 1
Homologous superfamily homologous superfamily	10 — Crystallins

Domain ID domain_id	1elpB02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	20 — Gamma-B Crystallin; domain 1
Homologous superfamily homologous superfamily	10 — Crystallins

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7. Citations (13)

Structure of bovine eye lens gammaD (gammaIIIb)-crystallin at 1.95 A.

Acta Crystallogr.,Sect.D (1996)

PMID: 15299634 · DOI: 10.1107/S0907444996000352 PRIMARY

Crystal Structure of Calf Eye Lens Gamma-Crystallin Iiib at 2.5 A Resolution: Its Relation to Function

Exp.Eye Res. (1991)

Surface Interactions of Gamma-Crystallins in the Crystal Medium in Relation to Their Association in the Eye Lens

Proteins (1988)

[the Key Role of the Residue 103 in the Surface Interactions of Gamma-Crystallins]

Mol.Biol.(Moscow) (1987)

Key Role of Residue 103 in Surface Interactions of Gamma-Crystallins

Mol.Biol.(Engl.Transl.) (1987)

Spatial Structure of Gamma-Crystallin Iiib from Calf Eye Lens at 2.5 Angstroms Resolution

Dokl.Akad.Nauk Sssr (1986)

Phase Improvement in Protein Crystallography Using a Mixed Electron Density Model

Acta Crystallogr.,Sect.A (1985)

Improvement of Protein Phases by Coarse Model Modification

Acta Crystallogr.,Sect.A (1984)

Structure of Gamma-Crystallin Iiib from the Eye Lens of the Calf at 3 Angstroms Resolution

Dokl.Akad.Nauk Sssr (1981)

Polypeptide Chain Pathway in Gamma-Crystallin Iiib from Calf Lens at 3 A Resolution

FEBS Lett. (1981)

Structure of Gamma-Crystallin Iiib from Calf Lens at 5 A Resolution

FEBS Lett. (1980)

Crystallographic Study of Gamma-Crystallins from Calf Lens

J.Mol.Biol. (1977)

Growing Single Crystals of Gamma Crystallin from the Calf Crystalline Lens

Dokl.Akad.Nauk Sssr (1976)

Unit-cell length a length_a	57.810 Å
Unit-cell length b length_b	70.030 Å
Unit-cell length c length_c	117.250 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	1.950 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	—
R_work r_work	0.2040
R_free r_free	—

Description description	GAMMA-D CRYSTALLIN
Molecular weight formula_weight	20778.2 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3146

GAMMA-D CRYSTALLIN STRUCTURE AT 1.95 A RESOLUTION

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

GAMMA-D CRYSTALLIN

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1elp__assembly_1__model_1

1elp__assembly_1__model_1 | I(q)

1elp__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (13)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	218

GAMMA-D CRYSTALLIN STRUCTURE AT 1.95 A RESOLUTION

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

GAMMA-D CRYSTALLIN

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1elp__assembly_1__model_1

1elp__assembly_1__model_1 | I(q)

1elp__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (13)