4v2o

Structure of saposin B in complex with chloroquine

Method: X-RAY DIFFRACTION Dmax: 79.6 Å Quality: GOOD

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

SAPOSIN-B

HOMO SAPIENS

UniProt P07602

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 195–273 Chain C; UniProt 195–273 Not recorded CLQ N4-(7-CHLORO-QUINOLIN-4-YL)-N1,N1-DIETHYL-PENTANE-1,4-DIAMINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;0.1M MES, PH 6.0, 30% PEG6000 Resolution 2.13 Å R-free 0.254
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 195–273 Not recorded CLQ N4-(7-CHLORO-QUINOLIN-4-YL)-N1,N1-DIETHYL-PENTANE-1,4-DIAMINE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;0.1M MES, PH 6.0, 30% PEG6000 Resolution 2.13 Å R-free 0.254

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.

20 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SAP_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–82; UniProt 195–273 Author chain B; PDBConstruct 4–82; UniProt 195–273 Author chain C; PDBConstruct 4–82; UniProt 195–273

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 4v2o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4v2o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4v2o
Deposition date deposition_date2014-10-13
Structure title titleStructure of saposin B in complex with chloroquine
Keywords keywordsHYDROLASE ACTIVATOR, PROTEIN-LIGAND COMPLEX; HYDROLASE ACTIVATOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.49
Radius of gyration Rg (electron density) rg_electron23.07
Forward intensity I(0) i014318900.00
Molecular weight molecular_weight26855.0 kDa
Excluded volume excluded_volume32981 ų
Envelope volume envelope_volume46654 ų
Hydration-shell volume shell_volume18484 ų
Envelope diameter envelope_diameter80.0
Shell Rg shell_rg27.61
Envelope Rg envelope_rg22.91
Shape Rg shape_rg23.09
Total Rg total_rg23.65
Total atoms total_atoms1850
Residues n_residues240
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 dmax79.6
Rg (real space) rg_real23.63
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real1.4320e+07
I(0) uncertainty (real space) i0_real_error2.1320e+05
Rg (reciprocal space) rg_reciprocal23.60
I(0) (reciprocal space) i0_reciprocal14320000.0000
Solution quality estimate total_estimate0.8341
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.7
Skewness Skewness skewness0.496
Kurtosis Kurtosis kurtosis-0.199
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha857600.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.640; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.959; Smooth: 0.961

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (5 domains)

Domain ID domain_idd4v2oa_
Class classa — All alpha proteins
Fold Fold folda.64 — Saposin-like
Superfamily Superfamily superfamilya.64.1 — Saposin
Family Family familya.64.1.3 — Saposin B
Domain ID domain_idd4v2ob1
Class classa — All alpha proteins
Fold Fold folda.64 — Saposin-like
Superfamily Superfamily superfamilya.64.1 — Saposin
Family Family familya.64.1.3 — Saposin B
Domain ID domain_idd4v2ob2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4v2oc1
Class classa — All alpha proteins
Fold Fold folda.64 — Saposin-like
Superfamily Superfamily superfamilya.64.1 — Saposin
Family Family familya.64.1.3 — Saposin B
Domain ID domain_idd4v2oc2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (3 domains)

Domain ID domain_id4v2oA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology225 — NK-Lysin
Homologous superfamily homologous superfamily10 — Saposin-like
Domain ID domain_id4v2oB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology225 — NK-Lysin
Homologous superfamily homologous superfamily10 — Saposin-like
Domain ID domain_id4v2oC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology225 — NK-Lysin
Homologous superfamily homologous superfamily10 — Saposin-like

8. Citations (1)

9. Files and Curves (10)