1qhf

YEAST PHOSPHOGLYCERATE MUTASE-3PG COMPLEX STRUCTURE TO 1.7 A

Method: X-RAY DIFFRACTION Dmax: 85.2 Å Quality: GOOD

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

PROTEIN (PHOSPHOGLYCERATE MUTASE)

OrganismNot specified

UniProt P00950

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–240 Chain B; UniProt 1–240 Not recorded SO4 SULFATE ION × 8 3PG 3-PHOSPHOGLYCERIC ACID × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.8;55% AMMONIUM SULFATE IN 10MM IMIDAZOLE BUFFER PH 6.8 WITH 1MM 3PG AND CONCENTRATION OF 10 MG ML PROTEIN Resolution 1.70 Å R-free 0.215

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.

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

View Construct and Data Evidence
UniProt name PMG1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–240; UniProt 1–240 Author chain B; PDBConstruct 1–240; UniProt 1–240

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 1qhf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1qhf
Deposition date deposition_date1999-05-13
Structure title titleYEAST PHOSPHOGLYCERATE MUTASE-3PG COMPLEX STRUCTURE TO 1.7 A
Keywords keywordsTRANSFERASE (PHOSPHORYL), TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.12
Radius of gyration Rg (electron density) rg_electron24.36
Forward intensity I(0) i048204800.00
Molecular weight molecular_weight54426.0 kDa
Excluded volume excluded_volume68453 ų
Envelope volume envelope_volume80663 ų
Hydration-shell volume shell_volume27769 ų
Envelope diameter envelope_diameter89.6
Shell Rg shell_rg31.37
Envelope Rg envelope_rg24.55
Shape Rg shape_rg24.37
Total Rg total_rg25.13
Total atoms total_atoms3840
Residues n_residues480
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 dmax85.2
Rg (real space) rg_real25.14
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real4.8200e+07
I(0) uncertainty (real space) i0_real_error7.4370e+05
Rg (reciprocal space) rg_reciprocal25.13
I(0) (reciprocal space) i0_reciprocal48200000.0000
Solution quality estimate total_estimate0.8749
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.0
Skewness Skewness skewness0.396
Kurtosis Kurtosis kurtosis-0.308
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13100000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.815; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.932; Smooth: 0.994

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_idd1qhfa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.60 — Phosphoglycerate mutase-like
Superfamily Superfamily superfamilyc.60.1 — Phosphoglycerate mutase-like
Family Family familyc.60.1.1 — Cofactor-dependent phosphoglycerate mutase
Domain ID domain_idd1qhfb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.60 — Phosphoglycerate mutase-like
Superfamily Superfamily superfamilyc.60.1 — Phosphoglycerate mutase-like
Family Family familyc.60.1.1 — Cofactor-dependent phosphoglycerate mutase

CATH v4.4 (2 domains)

Domain ID domain_id1qhfA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1240 — Phosphoglycerate mutase-like
Domain ID domain_id1qhfB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1240 — Phosphoglycerate mutase-like

8. Citations (1)

9. Files and Curves (10)