SAXSdb — 1q2h

▼

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

adaptor protein with pleckstrin homology and src homology 2 domains

Homo sapiens

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
2	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	APS_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–69； UniProt 21–85 Author chain B； PDBConstruct 5–69； UniProt 21–85 Author chain C； PDBConstruct 5–69； UniProt 21–85

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	1q2h
Deposition date deposition_date	2003-07-24
Structure title title	Phenylalanine Zipper Mediates APS Dimerization
Keywords keywords	signal transduction, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

▼

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.

1q2h__assembly_1__model_1

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

Download this curve (.dat)

1q2h__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1q2h__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	16.41 Å
Rg (electron density)	15.42 Å
Total Rg	16.53 Å
Atom count	1015
Residues	125
Excluded volume	17683 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1q2h__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1q2h__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (2)

▼

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1q2ha_
Class class	a — All alpha proteins
Fold Fold fold	a.34 — Dimerisation interlock
Superfamily Superfamily superfamily	a.34.4 — Phenylalanine zipper
Family Family family	a.34.4.1 — Adapter protein APS, dimerisation domain

Domain ID domain_id	d1q2hb_
Class class	a — All alpha proteins
Fold Fold fold	a.34 — Dimerisation interlock
Superfamily Superfamily superfamily	a.34.4 — Phenylalanine zipper
Family Family family	a.34.4.1 — Adapter protein APS, dimerisation domain

Domain ID domain_id	d1q2hc_
Class class	a — All alpha proteins
Fold Fold fold	a.34 — Dimerisation interlock
Superfamily Superfamily superfamily	a.34.4 — Phenylalanine zipper
Family Family family	a.34.4.1 — Adapter protein APS, dimerisation domain

CATH v4.4 (3 domains)

Domain ID domain_id	1q2hA00
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	140 — Helix Hairpins
Homologous superfamily homologous superfamily	110 —

Domain ID domain_id	1q2hB00
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	140 — Helix Hairpins
Homologous superfamily homologous superfamily	110 —

Domain ID domain_id	1q2hC00
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	140 — Helix Hairpins
Homologous superfamily homologous superfamily	110 —

▶

Unit-cell length a length_a	69.740 Å
Unit-cell length b length_b	57.480 Å
Unit-cell length c length_c	51.720 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	12

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	1.700 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	—
R_work r_work	0.2500
R_free r_free	0.2700

Description description	adaptor protein with pleckstrin homology and src homology 2 domains
Molecular weight formula_weight	7778.7 kDa
Source method src_method	man
Copy count entity_count	3

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	1592

Phenylalanine Zipper Mediates APS Dimerization

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

adaptor protein with pleckstrin homology and src homology 2 domains

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

1q2h__assembly_1__model_1

1q2h__assembly_1__model_1 | I(q)

1q2h__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) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 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 BL21(DE3)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	64

Phenylalanine Zipper Mediates APS Dimerization

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

adaptor protein with pleckstrin homology and src homology 2 domains

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

1q2h__assembly_1__model_1

1q2h__assembly_1__model_1 | I(q)

1q2h__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) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (1)