SAXSdb — 1fo6

▼

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

N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE

Agrobacterium tumefaciens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	XENON × 2 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	DCAS_9RHIZ
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–304； UniProt 1–304 Author chain B； PDBConstruct 1–304； UniProt 1–304 Author chain C； PDBConstruct 1–304； UniProt 1–304 Author chain D； PDBConstruct 1–304； UniProt 1–304

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1fo6
Deposition date deposition_date	2000-08-25
Structure title title	CRYSTAL STRUCTURE ANALYSIS OF N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE
Keywords keywords	four layer a/b fold, HYDROLASE; HYDROLASE
Experimental Method method	X-RAY DIFFRACTION

▼

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.

1fo6__assembly_1__model_1

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

Download this curve (.dat)

1fo6__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1fo6__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	30.81 Å
Rg (electron density)	30.01 Å
Total Rg	30.66 Å
Atom count	9566
Residues	1208
Excluded volume	169810 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1fo6__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE
Molecular weight formula_weight	34209.1 kDa
EC 编号 ec_number	3.4.22.12
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	10288

MTRQMILAVGQQGPIARAETREQVVGRLLDMLTNAASRGVNFIVFPELALTTFFPRWHFTDEAELDSFYETEMPGPVVRPLFETAAELGIGFNLGYAELVVEGGVKRRFNTSILVDKSGKIVGKYRKIHLPGHKEYEAYRPFQHLEKRYFEPGDLGFPVYDVDAAKMGMFICNDRRWPETWRVMGLKGAEIICGGYNTPTHNPPVPQHDHLTSFHHLLSMQAGSYQNGAWSAAAGKVGMEEGCMLLGHSCIVAPTGEIVALTTTLEDEVITAALDLDRCRELREHIFNFKAHRQPQHYGLIAEF

Source Source

Source organism organism	Agrobacterium tumefaciens
NCBI taxonomy ID ncbi_taxonomy_id	358
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	XENON
Molecular weight formula_weight	131.3 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	722

▼

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1fo6a_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.160 — Carbon-nitrogen hydrolase
Superfamily Superfamily superfamily	d.160.1 — Carbon-nitrogen hydrolase
Family Family family	d.160.1.2 — Carbamilase

Domain ID domain_id	d1fo6b_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.160 — Carbon-nitrogen hydrolase
Superfamily Superfamily superfamily	d.160.1 — Carbon-nitrogen hydrolase
Family Family family	d.160.1.2 — Carbamilase

Domain ID domain_id	d1fo6c_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.160 — Carbon-nitrogen hydrolase
Superfamily Superfamily superfamily	d.160.1 — Carbon-nitrogen hydrolase
Family Family family	d.160.1.2 — Carbamilase

Domain ID domain_id	d1fo6d_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.160 — Carbon-nitrogen hydrolase
Superfamily Superfamily superfamily	d.160.1 — Carbon-nitrogen hydrolase
Family Family family	d.160.1.2 — Carbamilase

CATH v4.4 (4 domains)

Domain ID domain_id	1fo6A00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	110 — Nitrilase/N-carbamoyl-D-aminoacid amidohydrolase
Homologous superfamily homologous superfamily	10 — Carbon-nitrogen hydrolase

Domain ID domain_id	1fo6B00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	110 — Nitrilase/N-carbamoyl-D-aminoacid amidohydrolase
Homologous superfamily homologous superfamily	10 — Carbon-nitrogen hydrolase

Domain ID domain_id	1fo6C00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	110 — Nitrilase/N-carbamoyl-D-aminoacid amidohydrolase
Homologous superfamily homologous superfamily	10 — Carbon-nitrogen hydrolase

Domain ID domain_id	1fo6D00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	110 — Nitrilase/N-carbamoyl-D-aminoacid amidohydrolase
Homologous superfamily homologous superfamily	10 — Carbon-nitrogen hydrolase

▶

Unit-cell length a length_a	70.230 Å
Unit-cell length b length_b	67.530 Å
Unit-cell length c length_c	137.480 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	96.12 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.950 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.1867
R_work r_work	—
R_free r_free	0.2393

CRYSTAL STRUCTURE ANALYSIS OF N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE

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

N-CARBAMoYL-D-AMINO-ACID 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

1fo6__assembly_1__model_1

1fo6__assembly_1__model_1 | I(q)

1fo6__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

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

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (2)

CRYSTAL STRUCTURE ANALYSIS OF N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE

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

N-CARBAMoYL-D-AMINO-ACID 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

1fo6__assembly_1__model_1

1fo6__assembly_1__model_1 | I(q)

1fo6__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

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

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (2)