SAXSdb — 2qec

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

Histone acetyltransferase HPA2 and related acetyltransferases

Corynebacterium glutamicum ATCC 13032

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	1,2-ETHANEDIOL × 18 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q8NQB1_CORGL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–204； UniProt 1–203

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	2qec
Deposition date deposition_date	2007-06-25
Structure title title	Crystal structure of histone acetyltransferase HPA2 and related acetyltransferase (NP_600742.1) from Corynebacterium glutamicum ATCC 13032 at 1.90 A resolution
Keywords keywords	;NP_600742.1, histone acetyltransferase HPA2 and related acetyltransferase, Acetyltransferase (GNAT) family, Structural Genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-2, TRANSFERASE ;; TRANSFERASE
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.

2qec__assembly_1__model_1

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

Download this curve (.dat)

2qec__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2qec__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	25.70 Å
Rg (electron density)	24.85 Å
Total Rg	25.79 Å
Atom count	2822
Residues	356
Excluded volume	50641 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2qec__assembly_1__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 (3)

Entity 1 Entity 1 polymer

Description description	Histone acetyltransferase HPA2 and related acetyltransferases
Molecular weight formula_weight	22255.5 kDa
Mutation mutation	A29T
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	1576

GMSPTVLPATQADFPKIVDVLVEAFANDPTFLRWIPQPDPGSAKLRALFELQIEKQYAVAGNIDVARDSEGEIVGVALWDRPDGNHSAKDQAAMLPRLVSIFGIKAAQVAWTDLSSARFHPKFPHWYLYTVATSSSARGTGVGSALLNHGIARAGDEAIYLEATSTRAAQLYNRLGFVPLGYIPSDDDGTPELAMWKPPAMPTV

Source Source

Source organism organism	Corynebacterium glutamicum ATCC 13032
NCBI taxonomy ID ncbi_taxonomy_id	196627
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	9

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	151

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6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	2qecA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	630 — Aminopeptidase
Homologous superfamily homologous superfamily	30 — Gcn5-related N-acetyltransferase (GNAT)

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Unit-cell length a length_a	79.070 Å
Unit-cell length b length_b	79.070 Å
Unit-cell length c length_c	181.260 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 65 2 2
Space-group number int_tables_number	179
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	27.640 Å
R factor r_factor	0.1950
R_work r_work	0.1930
R_free r_free	0.2420

Crystal structure of histone acetyltransferase HPA2 and related acetyltransferase (NP_600742.1) from Corynebacterium glutamicum ATCC 13032 at 1.90 A resolution

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

Histone acetyltransferase HPA2 and related acetyltransferases

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

2qec__assembly_1__model_1

2qec__assembly_1__model_1 | I(q)

2qec__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

7. Citations (1)

Crystal structure of histone acetyltransferase HPA2 and related acetyltransferase (NP_600742.1) from Corynebacterium glutamicum ATCC 13032 at 1.90 A resolution

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

Histone acetyltransferase HPA2 and related acetyltransferases

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

2qec__assembly_1__model_1

2qec__assembly_1__model_1 | I(q)

2qec__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

7. Citations (1)