SAXSdb — 1b0b

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

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 2–142	Non-standard monomer：Yes (specific site not provided by mmCIF)	CYN CYANIDE ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；pH 6.5	Resolution 1.43 Å R-free 0.170

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 1B0B	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1EBT HEMOGLOBIN I FROM THE CLAM LUCINA PECTINATA BOUND WITH CYANIDE Deposited 1998-11-04	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–142（142 aa）	Not recorded	CYN CYANIDE ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；pH 7.00	Resolution 1.90 Å
1FLP STRUCTURE OF THE SULFIDE-REACTIVE HEMOGLOBIN FROM THE CLAM LUCINA PECTINATA: CRYSTALLOGRAPHIC ANALYSIS AT 1.5 ANGSTROMS RESOLUTION Deposited 1994-05-16	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–142（142 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.50 Å
1MOH FERRIC MONOMERIC HEMOGLOBIN I (HB I) Deposited 1996-02-27	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–142（142 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 1 H2S HYDROSULFURIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.90 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	GLB1_LUCPE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–142； 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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1b0b
Deposition date deposition_date	1998-11-06
Structure title title	HEMOGLOBIN I FROM THE CLAM LUCINA PECTINATA, CYANIDE COMPLEX AT 100 KELVIN
Keywords keywords	HEMOPROTEIN, SULFIDE CARRIER, GLOBINS, OXYGEN TRANSPORT, OXYGEN STORAGE-TRANSPORT COMPLEX; OXYGEN STORAGE/TRANSPORT
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	15.59 Å
Radius of gyration Rg (electron density) rg_electron	14.17 Å
Forward intensity I(0) i0	4700870.00
Molecular weight molecular_weight	15457.0 kDa
Excluded volume excluded_volume	19248 Å³
Envelope volume envelope_volume	20781 Å³
Hydration-shell volume shell_volume	12514 Å³
Envelope diameter envelope_diameter	48.4 Å
Shell Rg shell_rg	19.84 Å
Envelope Rg envelope_rg	14.39 Å
Shape Rg shape_rg	14.12 Å
Total Rg total_rg	15.38 Å
Total atoms total_atoms	1087
Residues n_residues	141
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	49.1 Å
Rg (real space) rg_real	15.48 Å
Rg uncertainty (real space) rg_real_error	0.26 Å
I(0) (real space) i0_real	4.7010e+06
I(0) uncertainty (real space) i0_real_error	4.9150e+04
Rg (reciprocal space) rg_reciprocal	15.49 Å
I(0) (reciprocal space) i0_reciprocal	4701000.0000
Solution quality estimate total_estimate	0.8920
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	20.5 Å
Skewness Skewness skewness	0.107
Kurtosis Kurtosis kurtosis	-0.362
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	685500.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.868; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.994

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	HEMOGLOBIN
Molecular weight formula_weight	14829.7 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	1307

SLSAAQKDNVKSSWAKASAAWGTAGPEFFMALFDAHDDVFAKFSGLFSGAAKGTVKNTPEMAAQAQSFKGLVSNWVDNLDNAGALEGQCKTFAANHKARGISAGQLEAAFKVLAGFMKSYGGDEGAWTAVAGALMGMIRPDM

Entity 2 Entity 2 non-polymer

Description description	CYANIDE ION
Molecular weight formula_weight	26.0 kDa
Source method src_method	syn
Copy count entity_count	1

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	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	202

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1b0ba_
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 (1 domains)

Domain ID domain_id	1b0bA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	490 — Globin-like
Homologous superfamily homologous superfamily	10 — Globins

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8. Citations (1)

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Unit-cell length a length_a	49.440 Å
Unit-cell length b length_b	37.950 Å
Unit-cell length c length_c	41.370 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	106.19 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	2

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.430 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.1187
R_work r_work	—
R_free r_free	0.1698

fit	/app/data/saxs_computation/b0/1b0b/1b0b.fit
pddf	/app/data/pr_computation/b0/1b0b/1b0b.pr.out
profile	/app/data/saxs_computation/b0/1b0b/1b0b.dat

HEMOGLOBIN I FROM THE CLAM LUCINA PECTINATA, CYANIDE COMPLEX AT 100 KELVIN

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

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