SAXSdb — 2q7s

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

N-formylglutamate amidohydrolase

Ralstonia eutropha

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	ZINC ION × 1 water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	ZINC ION × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q46VW8_RALEJ
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–290； UniProt 1–289 Author chain B； PDBConstruct 2–290； UniProt 1–289

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	2q7s
Deposition date deposition_date	2007-06-07
Structure title title	Crystal structure of N-formylglutamate amidohydrolase (YP_297560.1) from Ralstonia eutropha JMP134 at 2.00 A resolution
Keywords keywords	;YP_297560.1, N-formylglutamate amidohydrolase, Structural Genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-2, HYDROLASE ;; HYDROLASE
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.

2q7s__assembly_1__model_1

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

Download this curve (.dat)

2q7s__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2q7s__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	19.24 Å
Rg (electron density)	18.30 Å
Total Rg	19.14 Å
Atom count	2145
Residues	268
Excluded volume	37986 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2q7s__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2q7s__assembly_2__model_1`	monomeric （1）	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	N-formylglutamate amidohydrolase
Molecular weight formula_weight	32882.4 kDa
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	4703

GMNQAMDTKQIAPFTLALPEGEALPLVCDSPHSGTFYPADFGAVVAPERLRGGEDTHVDALWEAVPRVGGTLLAATFPRVYIDPNRMLDDIDPAQLEGPWPTPLAPGEKTRLGYGLIWSNVDAATPIYDRKLTVAEVQRRINRYYRPYHAALTEAVEGAYQRFGAVWHLNLHSMPNNAYERLKIQSPRPLADFVLGDRDGTTCEPGLVDLVERELREKGYTVARNDPYKGVQLIAQIGRPAERRNSLQIEIRRPLYMEEGTRERNEGFATLQRDLTLLTLRIAEYVRRGV

Source Source

Source organism organism	Ralstonia eutropha
NCBI taxonomy ID ncbi_taxonomy_id	264198
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	297

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2q7sa1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.56 — Phosphorylase/hydrolase-like
Superfamily Superfamily superfamily	c.56.5 — Zn-dependent exopeptidases
Family Family family	c.56.5.9 — FGase-like

Domain ID domain_id	d2q7sb_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.56 — Phosphorylase/hydrolase-like
Superfamily Superfamily superfamily	c.56.5 — Zn-dependent exopeptidases
Family Family family	c.56.5.9 — FGase-like

CATH v4.4 (2 domains)

Domain ID domain_id	2q7sA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	630 — Aminopeptidase
Homologous superfamily homologous superfamily	40 — Zn-dependent exopeptidases

Domain ID domain_id	2q7sB00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	630 — Aminopeptidase
Homologous superfamily homologous superfamily	40 — Zn-dependent exopeptidases

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Unit-cell length a length_a	58.610 Å
Unit-cell length b length_b	74.835 Å
Unit-cell length c length_c	145.163 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	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	29.604 Å
R factor r_factor	0.2020
R_work r_work	0.1990
R_free r_free	0.2460

Crystal structure of N-formylglutamate amidohydrolase (YP_297560.1) from Ralstonia eutropha JMP134 at 2.00 A resolution

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

N-formylglutamate amidohydrolase

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

2q7s__assembly_1__model_1

2q7s__assembly_1__model_1 | I(q)

2q7s__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) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Crystal structure of N-formylglutamate amidohydrolase (YP_297560.1) from Ralstonia eutropha JMP134 at 2.00 A resolution

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

N-formylglutamate amidohydrolase

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

2q7s__assembly_1__model_1

2q7s__assembly_1__model_1 | I(q)

2q7s__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) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)