1cb6

STRUCTURE OF HUMAN APOLACTOFERRIN AT 2.0 A RESOLUTION.

Method: X-RAY DIFFRACTION Dmax: 92.3 Å Quality: REASONABLE

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

Lactotransferrin

OrganismNot specified

UniProt P02788

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 20–710 Fragment:UNP residues 20-710 CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.8;pH 7.8 Resolution 2.00 Å R-free 0.286

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.

26 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRFL_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–691; UniProt 20–710

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 1cb6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cb6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1cb6
Deposition date deposition_date1999-03-01
Structure title titleSTRUCTURE OF HUMAN APOLACTOFERRIN AT 2.0 A RESOLUTION.
Keywords keywordsIRON TRANSPORT, APOLACTOFERRIN, CONFORMATIONAL CHANGE; IRON TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.45
Radius of gyration Rg (electron density) rg_electron28.46
Forward intensity I(0) i0100268000.00
Molecular weight molecular_weight76246.0 kDa
Excluded volume excluded_volume94336 ų
Envelope volume envelope_volume115780 ų
Hydration-shell volume shell_volume34117 ų
Envelope diameter envelope_diameter98.6
Shell Rg shell_rg35.61
Envelope Rg envelope_rg28.41
Shape Rg shape_rg28.44
Total Rg total_rg29.16
Total atoms total_atoms5347
Residues n_residues691
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 dmax92.3
Rg (real space) rg_real29.41
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real1.0030e+08
I(0) uncertainty (real space) i0_real_error1.4810e+06
Rg (reciprocal space) rg_reciprocal29.43
I(0) (reciprocal space) i0_reciprocal100300000.0000
Solution quality estimate total_estimate0.7113
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.5
Skewness Skewness skewness0.250
Kurtosis Kurtosis kurtosis-0.545
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha20170000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 0.218; Positv: 1.000; Valcen: 0.999; Smooth: 0.728

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1cb6a1
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
Domain ID domain_idd1cb6a2
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 (4 domains)

Domain ID domain_id1cb6A01
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_id1cb6A02
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_id1cb6A03
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_id1cb6A04
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 (5)

9. Files and Curves (10)