SAXSdb — 6ypa

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

CN hydrolase domain-containing protein

Pyrococcus horikoshii

State in the Current Structure

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

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	O58376_PYRHO
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 21–282； UniProt 1–262 Author chain B； PDBConstruct 21–282； UniProt 1–262 Author chain C； PDBConstruct 21–282； UniProt 1–262 Author chain D； PDBConstruct 21–282； UniProt 1–262

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	6ypa
Deposition date deposition_date	2020-04-15
Structure title title	The C146A variant of an amidase from Pyrococcus horikoshii with bound glutaramide
Keywords keywords	amidase of the nitrilase superfamily, 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.

6ypa__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

6ypa__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

6ypa__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	25.76 Å
Rg (electron density)	24.81 Å
Total Rg	25.71 Å
Atom count	4248
Residues	527
Excluded volume	76423 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`6ypa__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`6ypa__assembly_2__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 (4)

Entity 1 Entity 1 polymer

Description description	CN hydrolase domain-containing protein
Molecular weight formula_weight	31983.7 kDa
Mutation mutation	C146A
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	9115

MGSSHHHHHHSSGLVPRGSHMVKVGYIQMEPKILELDKNYSKAEKLIKEASKEGAKLVVLPELFDTGYNFESREEVFDVAQQIPEGETTTFLMELARELGLYIVAGTAEKSGNYLYNSAVVVGPRGYIGKYRKIHLFYREKVFFEPGDLGFKVFDIGFAKVGVMIAFDWFFPESARTLALKGAEIIAHPANLVMPYAPRAMPIRALENRVYTITADRVGEERGLKFIGKSLIASPKAEVLSIASETEEEIGVVEIDLNLARNKRLNDMNDIFKDRREEYYFR

Source Source

Source organism organism	Pyrococcus horikoshii
NCBI taxonomy ID ncbi_taxonomy_id	53953
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 non-polymer

Description description	pentanediamide
Molecular weight formula_weight	130.1 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	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	556

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6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d6ypaa1
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	d6ypaa2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d6ypab1
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	d6ypab2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d6ypac1
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	d6ypac2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d6ypad1
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	d6ypad2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (4 domains)

Domain ID domain_id	6ypaA00
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	6ypaB00
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	6ypaC00
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	6ypaD00
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

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Unit-cell length a length_a	77.684 Å
Unit-cell length b length_b	100.639 Å
Unit-cell length c length_c	134.096 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	16

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	1.580 Å
Low-resolution limit resolution_low	80.492 Å
R factor r_factor	0.2082
R_work r_work	0.2065
R_free r_free	0.2398

The C146A variant of an amidase from Pyrococcus horikoshii with bound glutaramide

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

CN hydrolase domain-containing protein

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

6ypa__assembly_2__model_1

6ypa__assembly_2__model_1 | I(q)

6ypa__assembly_2__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 (4)

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 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (8 domains)

CATH v4.4 (4 domains)

7. Citations (1)

The C146A variant of an amidase from Pyrococcus horikoshii with bound glutaramide

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

CN hydrolase domain-containing protein

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

6ypa__assembly_2__model_1

6ypa__assembly_2__model_1 | I(q)

6ypa__assembly_2__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 (4)

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 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (8 domains)

CATH v4.4 (4 domains)

7. Citations (1)