SAXSdb — 2a8w

▼

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

;Histo-blood group ABO system transferase (NAGAT) [Includes: Glycoprotein-fucosylgalactoside alpha-N- acetylgalactosaminyltransferase (EC 2.4.1.40) (Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase) (Histo-blood group A transferase) (A transferase); Glycoprotein-fucosylgalactoside alpha- galactosyltransferase (EC 2.4.1.37) (Fucosylglycoprotein 3-alpha- galactosyltransferase) (Histo-blood group B transferase) (B transferase)] [Contains: Fucosylglycoprotein alpha-N- acetylgalactosaminyltransferase, soluble form] ;

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	MERCURY (II) ION × 5 CHLORIDE ION × 1 MANGANESE (II) ION × 1 URIDINE-5'-DIPHOSPHATE × 1 water × 1	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	MERCURY (II) ION × 10 CHLORIDE ION × 2 MANGANESE (II) ION × 2 URIDINE-5'-DIPHOSPHATE × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	BGAT_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–293； UniProt 64–354

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	2a8w
Deposition date deposition_date	2005-07-09
Structure title title	Crystal Structure of Human N-acetylgalactosaminyltransferase (GTA) Complexed with Beta-Methyllactoside
Keywords keywords	GTA, ABO(H), blood groups, glycosyltransferase, retaining, TRANSFERASE; TRANSFERASE
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.

2a8w__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2a8w__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2a8w__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	25.79 Å
Rg (electron density)	24.92 Å
Total Rg	25.60 Å
Atom count	4366
Residues	526
Excluded volume	78508 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2a8w__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2a8w__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 (6)

Entity 1 Entity 1 polymer

Description description	;Histo-blood group ABO system transferase (NAGAT) [Includes: Glycoprotein-fucosylgalactoside alpha-N- acetylgalactosaminyltransferase (EC 2.4.1.40) (Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase) (Histo-blood group A transferase) (A transferase); Glycoprotein-fucosylgalactoside alpha- galactosyltransferase (EC 2.4.1.37) (Fucosylglycoprotein 3-alpha- galactosyltransferase) (Histo-blood group B transferase) (B transferase)] [Contains: Fucosylglycoprotein alpha-N- acetylgalactosaminyltransferase, soluble form] ;
Molecular weight formula_weight	34194.5 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	2409

FMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRVTLGTGRQLSVLEVRAYKRWQDVSMRRMEMISDFCERRFLSEVDYLVCVDVDMEFRDHVGVEILTPLFGTLHPGFYGSSREAFTYERRPQSQAYIPKDEGDFYYLGGFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPKNHQAVRNP

Source Source

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

Entity 2 Entity 2 non-polymer

Description description	MERCURY (II) ION
Molecular weight formula_weight	200.6 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 3 Entity 3 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	MANGANESE (II) ION
Molecular weight formula_weight	54.9 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 non-polymer

Description description	URIDINE-5'-DIPHOSPHATE
Molecular weight formula_weight	404.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	226

▼

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2a8wa2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.68 — Nucleotide-diphospho-sugar transferases
Superfamily Superfamily superfamily	c.68.1 — Nucleotide-diphospho-sugar transferases
Family Family family	c.68.1.9 — alpha-1,3-galactosyltransferase-like

Domain ID domain_id	d2a8wa3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id	2a8wA00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	550 — Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
Homologous superfamily homologous superfamily	10 — Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

▶

Unit-cell length a length_a	52.620 Å
Unit-cell length b length_b	150.090 Å
Unit-cell length c length_c	79.550 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	8

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	1.590 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	—
R_work r_work	0.2100
R_free r_free	0.2320

Crystal Structure of Human N-acetylgalactosaminyltransferase (GTA) Complexed with Beta-Methyllactoside

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

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

2a8w__assembly_2__model_1

2a8w__assembly_2__model_1 | I(q)

2a8w__assembly_2__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 (6)

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 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

CATH v4.4 (1 domains)

7. Citations (1)

Crystal Structure of Human N-acetylgalactosaminyltransferase (GTA) Complexed with Beta-Methyllactoside

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

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

2a8w__assembly_2__model_1

2a8w__assembly_2__model_1 | I(q)

2a8w__assembly_2__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 (6)

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 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

CATH v4.4 (1 domains)

7. Citations (1)