4qaf

Crystal structure of an engineered lipocalin (Anticalin) in complex with VEGF(8-109)

Method: X-RAY DIFFRACTION Dmax: 95.2 Å Quality: GOOD

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

Lipocalin-1

Homo sapiens

UniProt P31025

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 23–174 Chain B; UniProt 23–174 Fragment:UNP residues 23-174 Mutation:;R26V,E27G,F28A,P29L,E30R,M31C,N32L,L33A,E34G,T37I,M39T,L56H,S58K,C61S,E69S,K76I,D80I,K83I,Y87K,I89G,C101S,E104C,H106S,K108V,R111P,K114W,C153S ; Vascular endothelial growth factor A × 2 (P15692) OMA 10-{(1R,2R)-2-[(2E)-hex-2-en-1-yl]cyclopropyl}decanoic acid × 2 SO4 SULFATE ION × 3 ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 3.5;293 K;1 M sodium chloride, 0.2 M lithium sulfate, 7.5% w/v dextran sulfate, pH 3.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.80 Å R-free 0.242

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.

3 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LCN1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–152; UniProt 23–174 Author chain B; PDBConstruct 1–152; UniProt 23–174

Vascular endothelial growth factor A

Homo sapiens

UniProt P15692

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 34–135 Chain D; UniProt 34–135 Fragment:UNP residues 34-135 Lipocalin-1 × 2 (P31025) OMA 10-{(1R,2R)-2-[(2E)-hex-2-en-1-yl]cyclopropyl}decanoic acid × 2 SO4 SULFATE ION × 3 ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 3.5;293 K;1 M sodium chloride, 0.2 M lithium sulfate, 7.5% w/v dextran sulfate, pH 3.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.80 Å R-free 0.242

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.

50 other PDB entries and 72 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VEGFA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–102; UniProt 34–135 Author chain D; PDBConstruct 1–102; UniProt 34–135

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 4qaf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4qaf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4qaf
Deposition date deposition_date2014-05-04
Structure title titleCrystal structure of an engineered lipocalin (Anticalin) in complex with VEGF(8-109)
Keywords keywordsbeta-barrel, binding protein, engineered lipocalin, TRANSPORT PROTEIN-SIGNALING PROTEIN complex; TRANSPORT PROTEIN/SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.78
Radius of gyration Rg (electron density) rg_electron28.14
Forward intensity I(0) i032413600.00
Molecular weight molecular_weight44285.0 kDa
Excluded volume excluded_volume55463 ų
Envelope volume envelope_volume71276 ų
Hydration-shell volume shell_volume22413 ų
Envelope diameter envelope_diameter95.8
Shell Rg shell_rg33.28
Envelope Rg envelope_rg28.33
Shape Rg shape_rg28.17
Total Rg total_rg28.59
Total atoms total_atoms3090
Residues n_residues389
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 dmax95.2
Rg (real space) rg_real28.12
Rg uncertainty (real space) rg_real_error0.99
I(0) (real space) i0_real3.2410e+07
I(0) uncertainty (real space) i0_real_error4.6680e+05
Rg (reciprocal space) rg_reciprocal28.02
I(0) (reciprocal space) i0_reciprocal32410000.0000
Solution quality estimate total_estimate0.8242
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.1
Skewness Skewness skewness0.556
Kurtosis Kurtosis kurtosis-0.357
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3688000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.699; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.696; Smooth: 0.924

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4qafc_
Class classg — Small proteins
Fold Fold foldg.17 — Cystine-knot cytokines
Superfamily Superfamily superfamilyg.17.1 — Cystine-knot cytokines
Family Family familyg.17.1.1 — Platelet-derived growth factor-like
Domain ID domain_idd4qafd_
Class classg — Small proteins
Fold Fold foldg.17 — Cystine-knot cytokines
Superfamily Superfamily superfamilyg.17.1 — Cystine-knot cytokines
Family Family familyg.17.1.1 — Platelet-derived growth factor-like

CATH v4.4 (2 domains)

Domain ID domain_id4qafC00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id4qafD00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines

8. Citations (1)

9. Files and Curves (10)