1iq7

Ovotransferrin, C-Terminal Lobe, Apo Form

Method: X-RAY DIFFRACTION Dmax: 65.5 Å Quality: EXCELLENT

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

Ovotransferrin

OrganismNot specified

UniProt P02789

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 361–705 Fragment:C-TERMINAL LOBE NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.30 Å R-free 0.239

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.

11 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRFE_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–345; UniProt 361–705

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 1iq7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1iq7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1iq7
Deposition date deposition_date2001-07-06
Structure title titleOvotransferrin, C-Terminal Lobe, Apo Form
Keywords keywordsTRANSFERRIN, OVOTRANSFERRIN, IRON BINDING PROTEIN, TRANSPORT PROTEIN, METAL TRANSPORT; METAL TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.00
Radius of gyration Rg (electron density) rg_electron20.85
Forward intensity I(0) i026997700.00
Molecular weight molecular_weight38213.0 kDa
Excluded volume excluded_volume47164 ų
Envelope volume envelope_volume55901 ų
Hydration-shell volume shell_volume22200 ų
Envelope diameter envelope_diameter67.5
Shell Rg shell_rg27.39
Envelope Rg envelope_rg20.84
Shape Rg shape_rg20.83
Total Rg total_rg21.72
Total atoms total_atoms2667
Residues n_residues341
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 dmax65.5
Rg (real space) rg_real21.88
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real2.7000e+07
I(0) uncertainty (real space) i0_real_error3.2950e+05
Rg (reciprocal space) rg_reciprocal21.90
I(0) (reciprocal space) i0_reciprocal27000000.0000
Solution quality estimate total_estimate0.9172
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.4
Skewness Skewness skewness0.148
Kurtosis Kurtosis kurtosis-0.587
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3875000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.977; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1iq7a_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamilyc.94.1 — Periplasmic binding protein-like II
Family Family familyc.94.1.2 — Transferrin

CATH v4.4 (2 domains)

Domain ID domain_id1iq7A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id1iq7A02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II

8. Citations (1)

9. Files and Curves (10)