2vfa

Crystal structure of a chimera of Plasmodium falciparum and human hypoxanthine-guanine phosphoribosyl transferases

Method: X-RAY DIFFRACTION Dmax: 85.0 Å Quality: GOOD

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

HYPOXANTHINE-GUANINE-XANTHINE PHOSPHORIBOSYLTRANSFERASE, HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE

PLASMODIUM FALCIPARUM

UniProt P00492

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 49–160 Chain B; UniProt 49–160 Fragment:RESIDUES 1-56,49-160,171-231 5GP GUANOSINE-5'-MONOPHOSPHATE × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;0.1M TRIS PH 8.0, 2.0M AMMONIUM SULPHATE Resolution 2.80 Å R-free 0.278

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.

23 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HPRT_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 57–168; UniProt 49–160 Author chain B; PDBConstruct 57–168; UniProt 49–160

HYPOXANTHINE-GUANINE-XANTHINE PHOSPHORIBOSYLTRANSFERASE, HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE

PLASMODIUM FALCIPARUM

UniProt P20035

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–56 Chain A; UniProt 171–231 Chain B; UniProt 1–56 Chain B; UniProt 171–231 Fragment:RESIDUES 1-56,49-160,171-231 5GP GUANOSINE-5'-MONOPHOSPHATE × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;0.1M TRIS PH 8.0, 2.0M AMMONIUM SULPHATE Resolution 2.80 Å R-free 0.278

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.

4 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HGXR_PLAFG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–56; UniProt 1–56 Author chain A; PDBConstruct 169–229; UniProt 171–231 Author chain B; PDBConstruct 1–56; UniProt 1–56 Author chain B; PDBConstruct 169–229; UniProt 171–231

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 2vfa

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2vfa
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2vfa
Deposition date deposition_date2007-11-02
Structure title titleCrystal structure of a chimera of Plasmodium falciparum and human hypoxanthine-guanine phosphoribosyl transferases
Keywords keywords;HYPOXANTHINE-GUANINE PHOSPHORIBOSYL TRANSFERASE (HGPRT), PURINE SALVAGE, DISEASE MUTATION, GLYCOSYLTRANSFERASE, TRANSFERASE, METAL-BINDING, GOUT, CHIMERA, MAGNESIUM ;; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.79
Radius of gyration Rg (electron density) rg_electron23.92
Forward intensity I(0) i031811600.00
Molecular weight molecular_weight44897.0 kDa
Excluded volume excluded_volume56836 ų
Envelope volume envelope_volume69197 ų
Hydration-shell volume shell_volume24642 ų
Envelope diameter envelope_diameter84.9
Shell Rg shell_rg30.36
Envelope Rg envelope_rg24.10
Shape Rg shape_rg23.90
Total Rg total_rg24.77
Total atoms total_atoms3160
Residues n_residues401
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 dmax85.0
Rg (real space) rg_real24.83
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real3.1810e+07
I(0) uncertainty (real space) i0_real_error5.1440e+05
Rg (reciprocal space) rg_reciprocal24.82
I(0) (reciprocal space) i0_reciprocal31810000.0000
Solution quality estimate total_estimate0.8714
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.0
Skewness Skewness skewness0.409
Kurtosis Kurtosis kurtosis-0.222
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8677000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.813; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.918; Smooth: 0.966

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2vfaa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.61 — PRTase-like
Superfamily Superfamily superfamilyc.61.1 — PRTase-like
Family Family familyc.61.1.1 — Phosphoribosyltransferases (PRTases)
Domain ID domain_idd2vfab_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.61 — PRTase-like
Superfamily Superfamily superfamilyc.61.1 — PRTase-like
Family Family familyc.61.1.1 — Phosphoribosyltransferases (PRTases)

CATH v4.4 (2 domains)

Domain ID domain_id2vfaA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2020
Domain ID domain_id2vfaB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2020

8. Citations (1)

9. Files and Curves (10)