1mas

PURINE NUCLEOSIDE HYDROLASE

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

INOSINE-URIDINE NUCLEOSIDE N-RIBOHYDROLASE

Crithidia fasciculata

UniProt Q27546

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 4 POTASSIUM ION × 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

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_id1mas
Deposition date deposition_date1995-12-18
Structure title titlePURINE NUCLEOSIDE HYDROLASE
Keywords keywordsHYDROLASE, PURINE NUCLEOSIDE HYDROLASE, PURINE NUCLEOSIDASE, IU-NH; HYDROLASE
Experimental Method methodX-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.

1mas__assembly_1__model_1

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

Download this curve (.dat)

1mas__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1mas__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)35.68 Å
Rg (electron density)34.95 Å
Total Rg35.39 Å
Atom count9240
Residues1206
Excluded volume166450 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1mas__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)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1masa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.70 — Nucleoside hydrolase
Superfamily Superfamily superfamilyc.70.1 — Nucleoside hydrolase
Family Family familyc.70.1.1 — Nucleoside hydrolase
Domain ID domain_idd1masb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.70 — Nucleoside hydrolase
Superfamily Superfamily superfamilyc.70.1 — Nucleoside hydrolase
Family Family familyc.70.1.1 — Nucleoside hydrolase

CATH v4.4 (2 domains)

Domain ID domain_id1masA00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology245 — Inosine-uridine Nucleoside N-ribohydrolase; Chain A
Homologous superfamily homologous superfamily10 — Ribonucleoside hydrolase-like
Domain ID domain_id1masB00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology245 — Inosine-uridine Nucleoside N-ribohydrolase; Chain A
Homologous superfamily homologous superfamily10 — Ribonucleoside hydrolase-like
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7. Citations (4)