SAXSdb — 1gzu

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

NICOTINAMIDE MONONUCLEOTIDE ADENYLYL TRANSFERASE

HOMO SAPIENS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 6	BETA-NICOTINAMIDE RIBOSE MONOPHOSPHATE × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9HAN9
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 13–290； UniProt 2–279 Author chain B； PDBConstruct 13–290； UniProt 2–279 Author chain C； PDBConstruct 13–290； UniProt 2–279

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	1gzu
Deposition date deposition_date	2002-06-06
Structure title title	Crystal Structure of Human Nicotinamide Mononucleotide Adenylyltransferase in Complex with NMN
Keywords keywords	TRANSFERASE, NAD BIOSYNTHESIS, ADENYLYLTRANSFERASE; 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.

1gzu__assembly_1__model_1

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

Download this curve (.dat)

1gzu__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1gzu__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	35.71 Å
Rg (electron density)	34.91 Å
Total Rg	35.54 Å
Atom count	11088
Residues	1350
Excluded volume	198870 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1gzu__assembly_1__model_1`	hexameric （6）	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) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1gzua_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.26 — Adenine nucleotide alpha hydrolase-like
Superfamily Superfamily superfamily	c.26.1 — Nucleotidylyl transferase
Family Family family	c.26.1.3 — Adenylyltransferase

Domain ID domain_id	d1gzub_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.26 — Adenine nucleotide alpha hydrolase-like
Superfamily Superfamily superfamily	c.26.1 — Nucleotidylyl transferase
Family Family family	c.26.1.3 — Adenylyltransferase

Domain ID domain_id	d1gzuc_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.26 — Adenine nucleotide alpha hydrolase-like
Superfamily Superfamily superfamily	c.26.1 — Nucleotidylyl transferase
Family Family family	c.26.1.3 — Adenylyltransferase

CATH v4.4 (3 domains)

Domain ID domain_id	1gzuA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	620 — HUPs

Domain ID domain_id	1gzuB00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	620 — HUPs

Domain ID domain_id	1gzuC00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	620 — HUPs

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Unit-cell length a length_a	140.800 Å
Unit-cell length b length_b	235.700 Å
Unit-cell length c length_c	89.000 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	24

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

Resolution resolution	2.900 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.2480
R_work r_work	0.2460
R_free r_free	0.2860

Description description	NICOTINAMIDE MONONUCLEOTIDE ADENYLYL TRANSFERASE
Molecular weight formula_weight	33444.4 kDa
EC 编号 ec_number	2.7.7.1
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	5544

Crystal Structure of Human Nicotinamide Mononucleotide Adenylyltransferase in Complex with NMN

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

NICOTINAMIDE MONONUCLEOTIDE ADENYLYL TRANSFERASE

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

1gzu__assembly_1__model_1

1gzu__assembly_1__model_1 | I(q)

1gzu__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 non-polymer

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

Description description	BETA-NICOTINAMIDE RIBOSE MONOPHOSPHATE
Molecular weight formula_weight	335.2 kDa
Source method src_method	syn
Copy count entity_count	3

Crystal Structure of Human Nicotinamide Mononucleotide Adenylyltransferase in Complex with NMN

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

NICOTINAMIDE MONONUCLEOTIDE ADENYLYL TRANSFERASE

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

1gzu__assembly_1__model_1

1gzu__assembly_1__model_1 | I(q)

1gzu__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 non-polymer

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (1)