SAXSdb — 1cg8

▼

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

PROTEIN (HEMOGLOBIN)

OrganismNot specified

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 2–142	Not recorded	PROTEIN (HEMOGLOBIN) × 2 （P56692） HEM PROTOPORPHYRIN IX CONTAINING FE × 4 CMO CARBON MONOXIDE × 4	X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；pH 6.5	Resolution 1.90 Å R-free 0.252

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 1CG8	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CG5 DEOXY FORM HEMOGLOBIN FROM DASYATIS AKAJEI Deposited 1999-03-26	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 2–142（141 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.5	Resolution 1.60 Å R-free 0.232

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	HBA_DASAK
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–141； UniProt 2–142

PROTEIN (HEMOGLOBIN)

OrganismNot specified

UniProt P56692

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain B； UniProt 2–142	Not recorded	PROTEIN (HEMOGLOBIN) × 2 （P56691） HEM PROTOPORPHYRIN IX CONTAINING FE × 4 CMO CARBON MONOXIDE × 4	X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；pH 6.5	Resolution 1.90 Å R-free 0.252

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 1CG8	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CG5 DEOXY FORM HEMOGLOBIN FROM DASYATIS AKAJEI Deposited 1999-03-26	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 2–142（141 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.5	Resolution 1.60 Å R-free 0.232

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	HBB_DASAK
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–141； UniProt 2–142

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1cg8
Deposition date deposition_date	1999-03-26
Structure title title	CO Form Hemoglobin from Dasyatis Akajei
Keywords keywords	OXYGEN TRANSPORT; OXYGEN TRANSPORT
Experimental Method method	X-RAY DIFFRACTION

▼

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

Radius of gyration Rg (Guinier) rg_guinier	20.75 Å
Radius of gyration Rg (electron density) rg_electron	19.44 Å
Forward intensity I(0) i0	18521100.00
Molecular weight molecular_weight	33415.0 kDa
Excluded volume excluded_volume	42131 Å³
Envelope volume envelope_volume	48554 Å³
Hydration-shell volume shell_volume	20680 Å³
Envelope diameter envelope_diameter	62.0 Å
Shell Rg shell_rg	25.95 Å
Envelope Rg envelope_rg	19.64 Å
Shape Rg shape_rg	19.41 Å
Total Rg total_rg	20.45 Å
Total atoms total_atoms	2362
Residues n_residues	282
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

▼

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

Maximum dimension Dmax dmax	62.2 Å
Rg (real space) rg_real	20.64 Å
Rg uncertainty (real space) rg_real_error	0.24 Å
I(0) (real space) i0_real	1.8520e+07
I(0) uncertainty (real space) i0_real_error	2.3320e+05
Rg (reciprocal space) rg_reciprocal	20.66 Å
I(0) (reciprocal space) i0_reciprocal	18520000.0000
Solution quality estimate total_estimate	0.9110
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	26.2 Å
Skewness Skewness skewness	0.159
Kurtosis Kurtosis kurtosis	-0.545
Angular range angular_range	— – 0.3850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3562000.0000
Real-space data points n_real_points	70
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.951; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.991

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	PROTEIN (HEMOGLOBIN)
Molecular weight formula_weight	15861.1 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2460

VLSSQNKKAIEELGNLIKANAEAWGADALARLFELHPQTKTYFSKFSGFEACNEQVKKHGKRVMNALADATHHLDNLHLHLEDLARKHGENLLVDPHNFHLFADCIVVTLAVNLQAFTPVTHCAVDKFLELVAYELSSCYR

Entity 2 Entity 2 polymer

Description description	PROTEIN (HEMOGLOBIN)
Molecular weight formula_weight	16315.6 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

VKLSEDQEHYIKGVWKDVDHKQITAKALERVFVVYPWTTRLFSKLQGLFSANDIGVQQHADKVQRALGEAIDDLKKVEINFQNLSGKHQEIGVDTQNFKLLGQTFMVELALHYKKTFRPKEHAAAYKFFRLVAEALSSNYH

Entity 3 Entity 3 non-polymer

Description description	PROTOPORPHYRIN IX CONTAINING FE
Molecular weight formula_weight	616.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	CARBON MONOXIDE
Molecular weight formula_weight	28.0 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	98

▼

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1cg8a_
Class class	a — All alpha proteins
Fold Fold fold	a.1 — Globin-like
Superfamily Superfamily superfamily	a.1.1 — Globin-like
Family Family family	a.1.1.2 — Globins

Domain ID domain_id	d1cg8b_
Class class	a — All alpha proteins
Fold Fold fold	a.1 — Globin-like
Superfamily Superfamily superfamily	a.1.1 — Globin-like
Family Family family	a.1.1.2 — Globins

CATH v4.4 (2 domains)

Domain ID domain_id	1cg8A00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	490 — Globin-like
Homologous superfamily homologous superfamily	10 — Globins

Domain ID domain_id	1cg8B00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	490 — Globin-like
Homologous superfamily homologous superfamily	10 — Globins

▶

8. Citations (1)

▶

Unit-cell length a length_a	57.660 Å
Unit-cell length b length_b	100.070 Å
Unit-cell length c length_c	107.610 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	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	6.000 Å
R factor r_factor	—
R_work r_work	0.1970
R_free r_free	0.2520

fit	/app/data/saxs_computation/cg/1cg8/1cg8.fit
pddf	/app/data/pr_computation/cg/1cg8/1cg8.pr.out
profile	/app/data/saxs_computation/cg/1cg8/1cg8.dat

CO Form Hemoglobin from Dasyatis Akajei

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

PROTEIN (HEMOGLOBIN)

State in the Current Structure

Other States of the Same Protein in the Database

PROTEIN (HEMOGLOBIN)

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

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

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 (1)

9. Files and Curves (10)

Files (7)

Curves (3)