SAXSdb — 28yl

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

3-oxoacyl-[acyl-carrier-protein] reductase FabG

Serratia plymuthica RVH1

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 4 GLYCEROL × 4 ISOPROPYL ALCOHOL × 2 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	T2I4E6_SERPL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–258； UniProt 1–255 Author chain B； PDBConstruct 4–258； UniProt 1–255 Author chain C； PDBConstruct 4–258； UniProt 1–255 Author chain D； PDBConstruct 4–258； UniProt 1–255

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	28yl
Deposition date deposition_date	2026-03-02
Last revision last_revision	2026-03-25
Structure title title	Crystal structure of the zeamine pathway ketoreductase Zmn13-KR, in complex with NADH
Keywords keywords	Short-chain dehydrogenase/reductase (SDR) superfamily, Rossmann fold, catalytic domain, NADH-dependent reduction, OXIDOREDUCTASE; 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.

28yl__assembly_1__model_1

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

Download this curve (.dat)

28yl__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

28yl__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	29.10 Å
Rg (electron density)	27.88 Å
Total Rg	28.61 Å
Atom count	7411
Residues	994
Excluded volume	131840 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`28yl__assembly_1__model_1`	tetrameric （4）	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	3-oxoacyl-[acyl-carrier-protein] reductase FabG
Molecular weight formula_weight	27078.0 kDa
EC 编号 ec_number	1.1.1.100
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,B,A,C
Atom count atom_count	7809

GSHMSHQVAVVTGAAGGFGTAIARVLLDIGYQVAAADVSAERLTQLAERLGHPEGLHTFVMDVTQEESIAQAAREIEARLGAALTVLVNNAGVIERSFCLSERGLSGAARVLNVNLLGTFNCTAVFSRYMARLKYGRIINIASIAGIWGAAGGSAYAASKAGVISATESWGRELGPLNISVTAVAPGICKTEMLAQFVDPHMIDTPEEEKIVRSIVPVGRWGTPEDVAEVVGFLASCKTNYLNTTVIPLDGGMRVGTL

Source Source

Source organism organism	Serratia plymuthica RVH1
NCBI taxonomy ID ncbi_taxonomy_id	1006598
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 non-polymer

Description description	1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE
Molecular weight formula_weight	665.4 kDa
Source method src_method	syn
Copy count entity_count	4

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	4

Entity 4 Entity 4 non-polymer

Description description	ISOPROPYL ALCOHOL
Molecular weight formula_weight	60.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	272

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Unit-cell length a length_a	80.342 Å
Unit-cell length b length_b	109.321 Å
Unit-cell length c length_c	208.278 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	32

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

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	64.739 Å
R factor r_factor	—
R_work r_work	0.1844
R_free r_free	0.2246

Crystal structure of the zeamine pathway ketoreductase Zmn13-KR, in complex with NADH

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

3-oxoacyl-[acyl-carrier-protein] reductase FabG

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

28yl__assembly_1__model_1

28yl__assembly_1__model_1 | I(q)

28yl__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

7. Citations (1)

Crystal structure of the zeamine pathway ketoreductase Zmn13-KR, in complex with NADH

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

3-oxoacyl-[acyl-carrier-protein] reductase FabG

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

28yl__assembly_1__model_1

28yl__assembly_1__model_1 | I(q)

28yl__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

7. Citations (1)