1lct

STRUCTURE OF THE RECOMBINANT N-TERMINAL LOBE OF HUMAN LACTOFERRIN AT 2.0 ANGSTROMS RESOLUTION

Method: X-RAY DIFFRACTION Dmax: 66.2 Å Quality: GOOD

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

LACTOFERRIN

Homo sapiens

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 21–353 Not recorded FE FE (III) ION × 1 CO3 CARBONATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.00 Å

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 1–333; UniProt 21–353

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 1lct

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1lct
Deposition date deposition_date1993-06-19
Structure title titleSTRUCTURE OF THE RECOMBINANT N-TERMINAL LOBE OF HUMAN LACTOFERRIN AT 2.0 ANGSTROMS RESOLUTION
Keywords keywordsIRON TRANSPORT; IRON TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.53
Radius of gyration Rg (electron density) rg_electron19.51
Forward intensity I(0) i022374900.00
Molecular weight molecular_weight35429.0 kDa
Excluded volume excluded_volume44062 ų
Envelope volume envelope_volume50505 ų
Hydration-shell volume shell_volume21437 ų
Envelope diameter envelope_diameter67.4
Shell Rg shell_rg26.07
Envelope Rg envelope_rg19.62
Shape Rg shape_rg19.50
Total Rg total_rg20.41
Total atoms total_atoms2494
Residues n_residues324
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 dmax66.2
Rg (real space) rg_real20.44
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real2.2370e+07
I(0) uncertainty (real space) i0_real_error2.8370e+05
Rg (reciprocal space) rg_reciprocal20.46
I(0) (reciprocal space) i0_reciprocal22380000.0000
Solution quality estimate total_estimate0.8913
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.0
Skewness Skewness skewness0.219
Kurtosis Kurtosis kurtosis-0.396
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4338000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.869; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.977

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_idd1lcta_
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_id1lctA01
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_id1lctA02
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 (4)

9. Files and Curves (10)