SAXSdb — 1q7s

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

bit1

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
3	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	PTH2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–117； UniProt 63–179 Author chain B； PDBConstruct 1–117； UniProt 63–179

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	1q7s
Deposition date deposition_date	2003-08-19
Structure title title	Crystal structure of bit1
Keywords keywords	APOPTOSIS; APOPTOSIS
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.

1q7s__assembly_1__model_1

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

Download this curve (.dat)

1q7s__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1q7s__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	15.04 Å
Rg (electron density)	13.72 Å
Total Rg	14.95 Å
Atom count	888
Residues	117
Excluded volume	16080 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1q7s__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1q7s__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1q7s__assembly_3__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) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1q7sa_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.131 — Peptidyl-tRNA hydrolase II
Superfamily Superfamily superfamily	c.131.1 — Peptidyl-tRNA hydrolase II
Family Family family	c.131.1.1 — Peptidyl-tRNA hydrolase II

Domain ID domain_id	d1q7sb_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.131 — Peptidyl-tRNA hydrolase II
Superfamily Superfamily superfamily	c.131.1 — Peptidyl-tRNA hydrolase II
Family Family family	c.131.1.1 — Peptidyl-tRNA hydrolase II

CATH v4.4 (2 domains)

Domain ID domain_id	1q7sA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1490 — Bit1
Homologous superfamily homologous superfamily	10 — Bit1

Domain ID domain_id	1q7sB00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1490 — Bit1
Homologous superfamily homologous superfamily	10 — Bit1

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Unit-cell length a length_a	61.861 Å
Unit-cell length b length_b	61.861 Å
Unit-cell length c length_c	178.135 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	16

Space group space_group	P 43 21 2
Space-group number int_tables_number	96
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	42.840 Å
R factor r_factor	0.2110
R_work r_work	0.2110
R_free r_free	0.2380

Description description	bit1
Molecular weight formula_weight	12697.9 kDa
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	1886

Crystal structure of bit1

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

bit1

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

1q7s__assembly_1__model_1

1q7s__assembly_1__model_1 | I(q)

1q7s__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

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	123

Crystal structure of bit1

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

bit1

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

1q7s__assembly_1__model_1

1q7s__assembly_1__model_1 | I(q)

1q7s__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

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)