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1dtz

STRUCTURE OF CAMEL APO-LACTOFERRIN DEMONSTRATES ITS DUAL ROLE IN SEQUESTERING AND TRANSPORTING FERRIC IONS SIMULTANEOUSLY:CRYSTAL STRUCTURE OF CAMEL APO-LACTOFERRIN AT 2.6A RESOLUTION.

Method: X-RAY DIFFRACTION Dmax: 98.1 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

APO LACTOFERRIN

OrganismNot specified

UniProt Q9TUM0

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 20–708 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：MICRODIALYSIS；pH 8；277 K；TRIS HCl ETHANOL TRISODIUM CITRATE, pH 8.0, MICRODIALYSIS, temperature 277K Resolution 2.65 Å R-free 0.266

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.

Other PDB Difference from Current Entry 1DTZ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1I6Q Formation of a protein intermediate and its trapping by the simultaneous crystallization process: Crystal structure of an iron-saturated intermediate in the FE3+ binding pathway of camel lactoferrin at 2.7 resolution Deposited 2001-03-03 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 20–708（689 aa）
Not recorded FE FE (III) ION × 2 CO3 CARBONATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions MICRODIALYSIS；pH 8；277 K；ethanol, pH 8.0, MICRODIALYSIS, temperature 277K
Resolution 2.70 Å R-free 0.255
2J4U E.coli OmpC - camel Lactoferrin complex Deposited 2006-09-06 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain S 20–64（45 aa） Fragment：N-TERM FRAGMENT, RESIDUES 20-64
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.99 Å R-free 0.282
2J4U E.coli OmpC - camel Lactoferrin complex Deposited 2006-09-06 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain X 20–64（45 aa） Fragment：N-TERM FRAGMENT, RESIDUES 20-64
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.99 Å R-free 0.282

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRFL_CAMDR
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–689； UniProt 20–708

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 1dtz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1dtz
Deposition date deposition_date2000-01-13
Structure title titleSTRUCTURE OF CAMEL APO-LACTOFERRIN DEMONSTRATES ITS DUAL ROLE IN SEQUESTERING AND TRANSPORTING FERRIC IONS SIMULTANEOUSLY:CRYSTAL STRUCTURE OF CAMEL APO-LACTOFERRIN AT 2.6A RESOLUTION.
Keywords keywordsCAMEL, LACTOFERRIN, APOLACTOFERRIN, TRANSFERRIN, MILK PROTEIN, METAL TRANSPORT; METAL TRANSPORT
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier30.87 Å
Radius of gyration Rg (electron density) rg_electron30.01 Å
Forward intensity I(0) i094255900.00
Molecular weight molecular_weight75369.0 kDa
Excluded volume excluded_volume93896 ų
Envelope volume envelope_volume116920 ų
Hydration-shell volume shell_volume33358 ų
Envelope diameter envelope_diameter103.3 Å
Shell Rg shell_rg36.16 Å
Envelope Rg envelope_rg29.78 Å
Shape Rg shape_rg29.98 Å
Total Rg total_rg30.65 Å
Total atoms total_atoms5284
Residues n_residues689
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax98.1 Å
Rg (real space) rg_real30.85 Å
Rg uncertainty (real space) rg_real_error0.82 Å
I(0) (real space) i0_real9.4260e+07
I(0) uncertainty (real space) i0_real_error1.6230e+06
Rg (reciprocal space) rg_reciprocal30.86 Å
I(0) (reciprocal space) i0_reciprocal94260000.0000
Solution quality estimate total_estimate0.9025
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.5 Å
Skewness Skewness skewness0.266
Kurtosis Kurtosis kurtosis-0.531
Angular range angular_range— – 0.2550 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13490000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.889
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1dtza1
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_idd1dtza2
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_id1dtzA01
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_id1dtzA02
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_id1dtzA03
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_id1dtzA04
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
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8. Citations (1)

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9. Files and Curves (10)