SAXSdb — 2mas

▼

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

INOSINE-URIDINE NUCLEOSIDE N-RIBOHYDROLASE

Crithidia fasciculata

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	CALCIUM ION × 4 2-(4-AMINO-PHENYL)-5-HYDROXYMETHYL-PYRROLIDINE-3,4-DIOL × 4 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	IUNH_CRIFA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–314； UniProt 2–314 Author chain B； PDBConstruct 2–314； UniProt 2–314 Author chain C； PDBConstruct 2–314； UniProt 2–314 Author chain D； PDBConstruct 2–314； UniProt 2–314

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	2mas
Deposition date deposition_date	1996-10-17
Structure title title	PURINE NUCLEOSIDE HYDROLASE WITH A TRANSITION STATE INHIBITOR
Keywords keywords	PURINE NUCLEOSIDE HYDROLASE, INOSINE, URIDINE, IU-NH, HYDROLASE, PURINE NUCLEOSIDASE; 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.

2mas__assembly_1__model_1

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

Download this curve (.dat)

2mas__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2mas__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	35.56 Å
Rg (electron density)	34.91 Å
Total Rg	35.33 Å
Atom count	9616
Residues	1252
Excluded volume	172860 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2mas__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 (4)

Entity 1 Entity 1 polymer

Description description	INOSINE-URIDINE NUCLEOSIDE N-RIBOHYDROLASE
Molecular weight formula_weight	34206.5 kDa
EC 编号 ec_number	3.2.2.1
Mutation mutation	P2A
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	9774

AKKIILDCDPGLDDAVAILLAHGNPEIELLAITTVVGNQTLAKVTRNAQLVADIAGITGVPIAAGCDKPLVRKIMTAGHIHGESGMGTVAYPAEFKNKVDERHAVNLIIDLVMSHEPKTITLVPTGGLTNIAMAARLEPRIVDRVKEVVLMGGGYHEGNATSVAEFNIIIDPEAAHIVFNESWQVTMVGLDLTHQALATPPILQRVKEVDTNPARFMLEIMDYYTKIYQSNRYMAAAAVHDPCAVAYVIDPSVMTTERVPVDIELTGKLTLGMTVADFRNPRPEHCHTQVAVKLDFEKFWGLVLDALERIGDPQ

Source Source

Source organism organism	Crithidia fasciculata
NCBI taxonomy ID ncbi_taxonomy_id	5656
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 non-polymer

Description description	2-(4-AMINO-PHENYL)-5-HYDROXYMETHYL-PYRROLIDINE-3,4-DIOL
Molecular weight formula_weight	224.3 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	158

▼

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d2masa_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.70 — Nucleoside hydrolase
Superfamily Superfamily superfamily	c.70.1 — Nucleoside hydrolase
Family Family family	c.70.1.1 — Nucleoside hydrolase

Domain ID domain_id	d2masb_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.70 — Nucleoside hydrolase
Superfamily Superfamily superfamily	c.70.1 — Nucleoside hydrolase
Family Family family	c.70.1.1 — Nucleoside hydrolase

Domain ID domain_id	d2masc_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.70 — Nucleoside hydrolase
Superfamily Superfamily superfamily	c.70.1 — Nucleoside hydrolase
Family Family family	c.70.1.1 — Nucleoside hydrolase

Domain ID domain_id	d2masd_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.70 — Nucleoside hydrolase
Superfamily Superfamily superfamily	c.70.1 — Nucleoside hydrolase
Family Family family	c.70.1.1 — Nucleoside hydrolase

CATH v4.4 (4 domains)

Domain ID domain_id	2masA00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	245 — Inosine-uridine Nucleoside N-ribohydrolase; Chain A
Homologous superfamily homologous superfamily	10 — Ribonucleoside hydrolase-like

Domain ID domain_id	2masB00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	245 — Inosine-uridine Nucleoside N-ribohydrolase; Chain A
Homologous superfamily homologous superfamily	10 — Ribonucleoside hydrolase-like

Domain ID domain_id	2masC00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	245 — Inosine-uridine Nucleoside N-ribohydrolase; Chain A
Homologous superfamily homologous superfamily	10 — Ribonucleoside hydrolase-like

Domain ID domain_id	2masD00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	245 — Inosine-uridine Nucleoside N-ribohydrolase; Chain A
Homologous superfamily homologous superfamily	10 — Ribonucleoside hydrolase-like

▶

Unit-cell length a length_a	120.630 Å
Unit-cell length b length_b	159.760 Å
Unit-cell length c length_c	206.380 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	32

Space group space_group	I 2 2 2
Space-group number int_tables_number	23
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	0.2050
R_work r_work	0.2050
R_free r_free	0.2340

PURINE NUCLEOSIDE HYDROLASE WITH A TRANSITION STATE INHIBITOR

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

INOSINE-URIDINE NUCLEOSIDE N-RIBOHYDROLASE

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

2mas__assembly_1__model_1

2mas__assembly_1__model_1 | I(q)

2mas__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 (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) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (2)

PURINE NUCLEOSIDE HYDROLASE WITH A TRANSITION STATE INHIBITOR

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

INOSINE-URIDINE NUCLEOSIDE N-RIBOHYDROLASE

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

2mas__assembly_1__model_1

2mas__assembly_1__model_1 | I(q)

2mas__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 (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) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (2)