SAXSdb — 1nba

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

N-CARBAMOYLSARCOSINE AMIDOHYDROLASE

Arthrobacter sp.

State in the Current Structure

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

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CSH_ARTSP
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–264； UniProt 1–264 Author chain B； PDBConstruct 1–264； UniProt 1–264 Author chain C； PDBConstruct 1–264； UniProt 1–264 Author chain D； PDBConstruct 1–264； UniProt 1–264

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	1nba
Deposition date deposition_date	1992-05-18
Structure title title	CRYSTAL STRUCTURE ANALYSIS, REFINEMENT AND ENZYMATIC REACTION MECHANISM OF N-CARBAMOYLSARCOSINE AMIDOHYDROLASE FROM ARTHROBACTER SP. AT 2.0 ANGSTROMS RESOLUTION
Keywords keywords	HYDROLASE(IN LINEAR AMIDES); HYDROLASE(IN LINEAR AMIDES)
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.

1nba__assembly_1__model_1

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

Download this curve (.dat)

1nba__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1nba__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	28.62 Å
Rg (electron density)	27.50 Å
Total Rg	28.28 Å
Atom count	7873
Residues	1011
Excluded volume	138570 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1nba__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 (3)

Entity 1 Entity 1 polymer

Description description	N-CARBAMOYLSARCOSINE AMIDOHYDROLASE
Molecular weight formula_weight	29084.3 kDa
EC 编号 ec_number	3.5.1.59
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	8304

MTETSGTFNDIEARLAAVLEEAFEAGTSIYNERGFKRRIGYGNRPAVIHIDLANAWTQPGHPFSCPGMETIIPNVQRINEAARAKGVPVFYTTNVYRNRDASSGTNDMGLWYSKIPTETLPADSYWAQIDDRIAPADGEVVIEKNRASAFPGTNLELFLTSNRIDTLIVTGATAAGCVRHTVEDAIAKGFRPIIPRETIGDRVPGVVQWNLYDIDNKFGDVESTDSVVQYLDALPQFEDTVPKTLSDPQPEVEAPADPVFAEQH

Source Source

Source organism organism	Arthrobacter sp.
NCBI taxonomy ID ncbi_taxonomy_id	1667

Entity 2 Entity 2 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	431

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1nbaa_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.33 — Isochorismatase-like hydrolases
Superfamily Superfamily superfamily	c.33.1 — Isochorismatase-like hydrolases
Family Family family	c.33.1.3 — Isochorismatase-like hydrolases

Domain ID domain_id	d1nbab_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.33 — Isochorismatase-like hydrolases
Superfamily Superfamily superfamily	c.33.1 — Isochorismatase-like hydrolases
Family Family family	c.33.1.3 — Isochorismatase-like hydrolases

Domain ID domain_id	d1nbac_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.33 — Isochorismatase-like hydrolases
Superfamily Superfamily superfamily	c.33.1 — Isochorismatase-like hydrolases
Family Family family	c.33.1.3 — Isochorismatase-like hydrolases

Domain ID domain_id	d1nbad_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.33 — Isochorismatase-like hydrolases
Superfamily Superfamily superfamily	c.33.1 — Isochorismatase-like hydrolases
Family Family family	c.33.1.3 — Isochorismatase-like hydrolases

CATH v4.4 (4 domains)

Domain ID domain_id	1nbaA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	850 — Isochorismatase-like

Domain ID domain_id	1nbaB00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	850 — Isochorismatase-like

Domain ID domain_id	1nbaC00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	850 — Isochorismatase-like

Domain ID domain_id	1nbaD00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	850 — Isochorismatase-like

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Unit-cell length a length_a	136.220 Å
Unit-cell length b length_b	122.290 Å
Unit-cell length c length_c	70.870 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	91.82 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	16

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

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	0.1860
R_work r_work	0.1860
R_free r_free	—

CRYSTAL STRUCTURE ANALYSIS, REFINEMENT AND ENZYMATIC REACTION MECHANISM OF N-CARBAMOYLSARCOSINE AMIDOHYDROLASE FROM ARTHROBACTER SP. AT 2.0 ANGSTROMS RESOLUTION

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

N-CARBAMOYLSARCOSINE 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

1nba__assembly_1__model_1

1nba__assembly_1__model_1 | I(q)

1nba__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 (1)

CRYSTAL STRUCTURE ANALYSIS, REFINEMENT AND ENZYMATIC REACTION MECHANISM OF N-CARBAMOYLSARCOSINE AMIDOHYDROLASE FROM ARTHROBACTER SP. AT 2.0 ANGSTROMS RESOLUTION

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

N-CARBAMOYLSARCOSINE 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

1nba__assembly_1__model_1

1nba__assembly_1__model_1 | I(q)

1nba__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 (1)