1un4

CRYSTAL STRUCTURE OF HUMAN ANGIOGENIN VARIANT T80A

Method: X-RAY DIFFRACTION Dmax: 49.4 Å Quality: GOOD

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

ANGIOGENIN

HOMO SAPIENS

UniProt P03950

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 25–147 Mutation:YES Non-standard monomer:Yes (specific site not provided by mmCIF) CIT CITRIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.2;15% PEG 4000, 0.02% DIOXANE, 0.2M SODIUM POTASSIUM TARTRATE, 0.02M SODIUM CITRATE BUFFER, PH 5.2 Resolution 2.10 Å R-free 0.232

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

53 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ANGI_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–123; UniProt 25–147

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.

SAXS scattering curve SAXS Profile

SAXS profile for 1un4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1un4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1un4
Deposition date deposition_date2003-09-04
Structure title titleCRYSTAL STRUCTURE OF HUMAN ANGIOGENIN VARIANT T80A
Keywords keywordsRIBONUCLEASE, HYDROLASE, NUCLEASE, ENDONUCLEASE, ANGIOGENESIS, PYRROLIDONE CARBOXYLIC ACID; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier15.35
Radius of gyration Rg (electron density) rg_electron14.24
Forward intensity I(0) i03907130.00
Molecular weight molecular_weight13181.0 kDa
Excluded volume excluded_volume16104 ų
Envelope volume envelope_volume18693 ų
Hydration-shell volume shell_volume11505 ų
Envelope diameter envelope_diameter48.2
Shell Rg shell_rg19.47
Envelope Rg envelope_rg14.44
Shape Rg shape_rg14.23
Total Rg total_rg15.27
Total atoms total_atoms926
Residues n_residues121
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax49.4
Rg (real space) rg_real15.29
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real3.9070e+06
I(0) uncertainty (real space) i0_real_error4.5520e+04
Rg (reciprocal space) rg_reciprocal15.30
I(0) (reciprocal space) i0_reciprocal3907000.0000
Solution quality estimate total_estimate0.8942
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.2
Skewness Skewness skewness0.238
Kurtosis Kurtosis kurtosis-0.393
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha789600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.880; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.982

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1un4a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.5 — RNase A-like
Superfamily Superfamily superfamilyd.5.1 — RNase A-like
Family Family familyd.5.1.1 — Ribonuclease A-like

CATH v4.4 (1 domains)

Domain ID domain_id1un4A00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology130 — P-30 Protein
Homologous superfamily homologous superfamily10 — Ribonuclease A-like domain

8. Citations (3)

9. Files and Curves (10)