1ki0

The X-ray Structure of Human Angiostatin

Method: X-RAY DIFFRACTION Dmax: 75.8 Å Quality: GOOD

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

ANGIOSTATIN

Homo sapiens

UniProt P00747

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 100–352 Mutation:N289E BCN BICINE × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;277 K;PEG 20,000, bicine, dioxane, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.75 Å R-free 0.263

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.

46 other PDB entries and 76 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PLMN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–253; UniProt 100–352

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 1ki0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ki0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ki0
Deposition date deposition_date2001-12-02
Structure title titleThe X-ray Structure of Human Angiostatin
Keywords keywordskringle domains, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.94
Radius of gyration Rg (electron density) rg_electron22.44
Forward intensity I(0) i018152100.00
Molecular weight molecular_weight29404.0 kDa
Excluded volume excluded_volume35492 ų
Envelope volume envelope_volume44240 ų
Hydration-shell volume shell_volume17608 ų
Envelope diameter envelope_diameter79.6
Shell Rg shell_rg27.51
Envelope Rg envelope_rg22.09
Shape Rg shape_rg22.47
Total Rg total_rg23.02
Total atoms total_atoms2054
Residues n_residues253
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 dmax75.8
Rg (real space) rg_real22.96
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real1.8150e+07
I(0) uncertainty (real space) i0_real_error2.7420e+05
Rg (reciprocal space) rg_reciprocal22.95
I(0) (reciprocal space) i0_reciprocal18150000.0000
Solution quality estimate total_estimate0.8046
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary32.6
Skewness Skewness skewness0.245
Kurtosis Kurtosis kurtosis-0.582
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4321000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.862; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.872; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1ki0a1
Class classg — Small proteins
Fold Fold foldg.14 — Kringle-like
Superfamily Superfamily superfamilyg.14.1 — Kringle-like
Family Family familyg.14.1.1 — Kringle modules
Domain ID domain_idd1ki0a2
Class classg — Small proteins
Fold Fold foldg.14 — Kringle-like
Superfamily Superfamily superfamilyg.14.1 — Kringle-like
Family Family familyg.14.1.1 — Kringle modules
Domain ID domain_idd1ki0a3
Class classg — Small proteins
Fold Fold foldg.14 — Kringle-like
Superfamily Superfamily superfamilyg.14.1 — Kringle-like
Family Family familyg.14.1.1 — Kringle modules

CATH v4.4 (3 domains)

Domain ID domain_id1ki0A01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology20 — Plasminogen Kringle 4
Homologous superfamily homologous superfamily10 — Plasminogen Kringle 4
Domain ID domain_id1ki0A02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology20 — Plasminogen Kringle 4
Homologous superfamily homologous superfamily10 — Plasminogen Kringle 4
Domain ID domain_id1ki0A03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology20 — Plasminogen Kringle 4
Homologous superfamily homologous superfamily10 — Plasminogen Kringle 4

8. Citations (1)

9. Files and Curves (10)