SAXSdb — 1gve

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

AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 3

RATTUS NORVEGICUS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 GLYCEROL × 12 CITRIC ACID × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	AR71_RAT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–327； UniProt 1–327 Author chain B； PDBConstruct 1–327； UniProt 1–327

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	1gve
Deposition date deposition_date	2002-02-08
Structure title title	Aflatoxin aldehyde reductase (AKR7A1) from Rat Liver
Keywords keywords	OXIDOREDUCTASE, ALDO-KETO REDUCTASE, AFLATOXIN B1, SUCCINIC SEMIALDEHYDE OXIDOREDUCTASE, AKR7 FAMILY; OXIDOREDUCTASE
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.

1gve__assembly_1__model_1

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

Download this curve (.dat)

1gve__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1gve__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	28.11 Å
Rg (electron density)	27.19 Å
Total Rg	28.07 Å
Atom count	5028
Residues	625
Excluded volume	89359 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1gve__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 (5)

Entity 1 Entity 1 polymer

Description description	AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 3
Molecular weight formula_weight	36790.0 kDa
EC 编号 ec_number	1.-.-.-
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	5567

MSQARPATVLGAMEMGRRMDVTSSSASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLGRSGCKVKIATKAAPMFGKTLKPADVRFQLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKNGWIMPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGRYKYQDKDGKNPESRFFGNPFSQLYMDRYWKEEHFNGIALVEKALKTTYGPTAPSMISAAVRWMYHHSQLKGTQGDAVILGMSSLEQLEQNLALVEEGPLEPAVVDAFDQAWNLVAHECPNYFR

Source Source

Source organism organism	RATTUS NORVEGICUS
Common name common_name	NORWAY RAT
NCBI taxonomy ID ncbi_taxonomy_id	10116
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
Molecular weight formula_weight	743.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	12

Entity 4 Entity 4 non-polymer

Description description	CITRIC ACID
Molecular weight formula_weight	192.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	504

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1gvea_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.7 — NAD(P)-linked oxidoreductase
Family Family family	c.1.7.1 — Aldo-keto reductases (NADP)

Domain ID domain_id	d1gveb_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.7 — NAD(P)-linked oxidoreductase
Family Family family	c.1.7.1 — Aldo-keto reductases (NADP)

CATH v4.4 (2 domains)

Domain ID domain_id	1gveA00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	100 — NADP-dependent oxidoreductase domain

Domain ID domain_id	1gveB00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	100 — NADP-dependent oxidoreductase domain

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Unit-cell length a length_a	125.540 Å
Unit-cell length b length_b	64.680 Å
Unit-cell length c length_c	112.840 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	91.03 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	1.380 Å
Low-resolution limit resolution_low	28.750 Å
R factor r_factor	0.1590
R_work r_work	0.1580
R_free r_free	0.1800

Aflatoxin aldehyde reductase (AKR7A1) from Rat Liver

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

AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 3

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

1gve__assembly_1__model_1

1gve__assembly_1__model_1 | I(q)

1gve__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 (5)

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 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (2)

Aflatoxin aldehyde reductase (AKR7A1) from Rat Liver

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

AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 3

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

1gve__assembly_1__model_1

1gve__assembly_1__model_1 | I(q)

1gve__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 (5)

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 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (2)