SAXSdb — 1hsy

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

MYOGLOBIN

Equus caballus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	SULFATE ION × 1 PROTOPORPHYRIN IX CONTAINING FE × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MYG_HORSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–153； UniProt 1–153

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	1hsy
Deposition date deposition_date	1994-12-12
Structure title title	ORIGIN OF THE PH-DEPENDENT SPECTROSCOPIC PROPERTIES OF PENTACOORDINATE METMYOGLOBIN VARIANTS
Keywords keywords	OXYGEN TRANSPORT; OXYGEN TRANSPORT
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.

1hsy__assembly_1__model_1

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

Download this curve (.dat)

1hsy__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1hsy__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	16.75 Å
Rg (electron density)	15.23 Å
Total Rg	16.43 Å
Atom count	1244
Residues	153
Excluded volume	22284 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1hsy__assembly_1__model_1`	monomeric （1）	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 (4)

Entity 1 Entity 1 polymer

Description description	MYOGLOBIN
Molecular weight formula_weight	16946.5 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1297

GLSDGEWQQVLNVWGKVEADIAGHGQEVLIRLFTGHPETLEKFDKFKHLKTEAEMKASEDLKKTGTVVLTALGGILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISDAIIHVLHSKHPGDFGADAQGAMTKALELFRNDIAAKYKELGFQG

Source Source

Source organism organism	Equus caballus
Common name common_name	horse
NCBI taxonomy ID ncbi_taxonomy_id	9796

Entity 2 Entity 2 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 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	53

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1hsya_
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	1hsyA00
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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7. Citations (9)

Origin of the pH-dependent spectroscopic properties of pentacoordinate metmyoglobin variants.

Biochemistry (1995)

PMID: 7654702 · DOI: 10.1021/bi00033a021 PRIMARY

Structural Characterization of Heme Ligation in the His64->Tyr Variant of Myoglobin

J.Biol.Chem. (1994)

Ftir Analysis of the Interaction of Azide with Horse Heart Myoglobin

Biochemistry (1994)

Three-Dimensional Structure of Cyanomet-Sulfmyoglobin C

Proc.Natl.Acad.Sci.USA (1994)

Expression in Escherichia Coli of a Synthetic Gene Coding for Horse Heart Myoglobin

Protein Eng. (1991)

High-Resolution Study of the Three-Dimensional Structure of Horse Heart Myoglobin

J.Mol.Biol. (1990)

Horse Heart Metmyoglobin: A 2.8-Angstroms Resolution Three-Dimensional Structure Determination

J.Biol.Chem. (1988)

Crystallization and Preliminary Diffraction Data for Horse Heart Metmyoglobin

J.Mol.Biol. (1987)

Thermal Destabilization of Horse Heart Myoglobin Through Modification of a Hydrophobic Cluster in the Proximal Heme Pocket

To be Published

Unit-cell length a length_a	64.403 Å
Unit-cell length b length_b	28.856 Å
Unit-cell length c length_c	35.790 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	107.20 °
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	1.900 Å
Low-resolution limit resolution_low	6.000 Å
R factor r_factor	0.1630
R_work r_work	—
R_free r_free	—

ORIGIN OF THE PH-DEPENDENT SPECTROSCOPIC PROPERTIES OF PENTACOORDINATE METMYOGLOBIN VARIANTS

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

MYOGLOBIN

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

1hsy__assembly_1__model_1

1hsy__assembly_1__model_1 | I(q)

1hsy__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (9)

ORIGIN OF THE PH-DEPENDENT SPECTROSCOPIC PROPERTIES OF PENTACOORDINATE METMYOGLOBIN VARIANTS

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

MYOGLOBIN

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

1hsy__assembly_1__model_1

1hsy__assembly_1__model_1 | I(q)

1hsy__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (9)