SAXSdb — 2g0b

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

FeeM

uncultured bacterium

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	N-DODECANOYL-L-TYROSINE × 1 water × 1	Consistent with protein count
10	Protein homooligomer	Homooligomer	Protein 2	N-DODECANOYL-L-TYROSINE × 2 water × 1	Consistent with protein count
11	Protein homooligomer	Homooligomer	Protein 2	N-DODECANOYL-L-TYROSINE × 2	Consistent with protein count
12	Protein homooligomer	Homooligomer	Protein 2	N-DODECANOYL-L-TYROSINE × 2	Consistent with protein count
13	Protein homooligomer	Homooligomer	Protein 2	N-DODECANOYL-L-TYROSINE × 2	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	N-DODECANOYL-L-TYROSINE × 1	Consistent with protein count
3	Protein monomer	Monomer	Protein 1	N-DODECANOYL-L-TYROSINE × 1	Consistent with protein count
4	Protein monomer	Monomer	Protein 1	N-DODECANOYL-L-TYROSINE × 1	Consistent with protein count
5	Protein monomer	Monomer	Protein 1	N-DODECANOYL-L-TYROSINE × 1	Consistent with protein count
6	Protein monomer	Monomer	Protein 1	N-DODECANOYL-L-TYROSINE × 1	Consistent with protein count
7	Protein monomer	Monomer	Protein 1	N-DODECANOYL-L-TYROSINE × 1	Consistent with protein count
8	Protein monomer	Monomer	Protein 1	N-DODECANOYL-L-TYROSINE × 1	Consistent with protein count
9	Protein homooligomer	Homooligomer	Protein 4	N-DODECANOYL-L-TYROSINE × 4 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q8KNZ7_9BACT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–198； UniProt 1–196 Author chain B； PDBConstruct 3–198； UniProt 1–196 Author chain C； PDBConstruct 3–198； UniProt 1–196 Author chain D； PDBConstruct 3–198； UniProt 1–196 Author chain E； PDBConstruct 3–198； UniProt 1–196 Author chain F； PDBConstruct 3–198； UniProt 1–196 Author chain G； PDBConstruct 3–198； UniProt 1–196 Author chain H； PDBConstruct 3–198； UniProt 1–196

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	2g0b
Deposition date deposition_date	2006-02-11
Structure title title	The structure of FeeM, an N-acyl amino acid synthase from uncultured soil microbes
Keywords keywords	N-acyl transferase, environmental DNA, protein-product complex, antibiotic synthase, 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.

2g0b__assembly_1__model_1

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

Download this curve (.dat)

2g0b__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2g0b__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	17.64 Å
Rg (electron density)	16.11 Å
Total Rg	17.32 Å
Atom count	1487
Residues	188
Excluded volume	26704 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2g0b__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2g0b__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2g0b__assembly_3__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`2g0b__assembly_4__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`2g0b__assembly_5__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
6	1	`2g0b__assembly_6__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
7	1	`2g0b__assembly_7__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
8	1	`2g0b__assembly_8__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
9	1	`2g0b__assembly_9__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
10	1	`2g0b__assembly_10__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
11	1	`2g0b__assembly_11__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
12	1	`2g0b__assembly_12__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
13	1	`2g0b__assembly_13__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	FeeM
Molecular weight formula_weight	21780.7 kDa
EC 编号 ec_number	2.3.1.-
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H
Atom count atom_count	11507

GSMTPRKVARILVAPNERDAARRIVRTTYEAQGYAIDESFATFLEGPSATTFGLFNGEVLYGTISIINDGAQGLPMDSIYAVELAAWRGEGKKLAEVVQFAMDHTLYEAVAGAKPSPFEAASLFTMVLTYALETHIDYLCISINPKHDTFYSLLGFTQIGALKHYGTVNAPAIARALYVPEWRSQTLLAQFMDAERSH

Source Source

Source organism organism	uncultured bacterium
NCBI taxonomy ID ncbi_taxonomy_id	77133
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 non-polymer

Description description	N-DODECANOYL-L-TYROSINE
Molecular weight formula_weight	363.5 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	9

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6. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id	2g0bA01
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)

Domain ID domain_id	2g0bB01
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)

Domain ID domain_id	2g0bC01
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)

Domain ID domain_id	2g0bD01
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)

Domain ID domain_id	2g0bE01
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)

Domain ID domain_id	2g0bF01
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)

Domain ID domain_id	2g0bG00
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)

Domain ID domain_id	2g0bH01
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	182.832 Å
Unit-cell length b length_b	182.832 Å
Unit-cell length c length_c	287.429 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	128

Space group space_group	I 41 2 2
Space-group number int_tables_number	98
Crystal system crystal_system	—

Resolution resolution	3.000 Å
Low-resolution limit resolution_low	29.750 Å
R factor r_factor	—
R_work r_work	0.2550
R_free r_free	0.2920

The structure of FeeM, an N-acyl amino acid synthase from uncultured soil microbes

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

FeeM

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

2g0b__assembly_1__model_1

2g0b__assembly_1__model_1 | I(q)

2g0b__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 (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) 8 domains

CATH v4.4 (8 domains)

7. Citations (1)

The structure of FeeM, an N-acyl amino acid synthase from uncultured soil microbes

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

FeeM

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

2g0b__assembly_1__model_1

2g0b__assembly_1__model_1 | I(q)

2g0b__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 (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) 8 domains

CATH v4.4 (8 domains)

7. Citations (1)