5pgm

SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE

Method: X-RAY DIFFRACTION Dmax: 167.6 Å Quality: REASONABLE

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

PHOSPHOGLYCERATE MUTASE 1

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 1–246 Chain B; UniProt 1–246 Chain C; UniProt 1–246 Chain D; UniProt 1–246 Not recorded SO4 SULFATE ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.65;pH 8.65 Resolution 2.12 Å R-free 0.228
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 1–246 Chain F; UniProt 1–246 Chain G; UniProt 1–246 Chain H; UniProt 1–246 Not recorded SO4 SULFATE ION × 8 ALA ALANINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.65;pH 8.65 Resolution 2.12 Å R-free 0.228

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 5 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 1–246; UniProt 1–246 Author chain B; PDBConstruct 1–246; UniProt 1–246 Author chain C; PDBConstruct 1–246; UniProt 1–246 Author chain D; PDBConstruct 1–246; UniProt 1–246 Author chain E; PDBConstruct 1–246; UniProt 1–246 Author chain F; PDBConstruct 1–246; UniProt 1–246 Author chain G; PDBConstruct 1–246; UniProt 1–246 Author chain H; PDBConstruct 1–246; UniProt 1–246

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 5pgm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5pgm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5pgm
Deposition date deposition_date1998-08-19
Structure title titleSACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE
Keywords keywordsISOMERASE, TRANSFERASE (PHOSPHORYL), GLYCOLYTIC ENZYME; ISOMERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier48.04
Radius of gyration Rg (electron density) rg_electron48.25
Forward intensity I(0) i0633237000.00
Molecular weight molecular_weight213120.0 kDa
Excluded volume excluded_volume268710 ų
Envelope volume envelope_volume358770 ų
Hydration-shell volume shell_volume64055 ų
Envelope diameter envelope_diameter178.8
Shell Rg shell_rg50.10
Envelope Rg envelope_rg47.50
Shape Rg shape_rg48.24
Total Rg total_rg48.34
Total atoms total_atoms15054
Residues n_residues1877
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 dmax167.6
Rg (real space) rg_real48.51
Rg uncertainty (real space) rg_real_error1.11
I(0) (real space) i0_real6.3340e+08
I(0) uncertainty (real space) i0_real_error1.1320e+07
Rg (reciprocal space) rg_reciprocal48.04
I(0) (reciprocal space) i0_reciprocal632900000.0000
Solution quality estimate total_estimate0.6101
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.7
Skewness Skewness skewness0.455
Kurtosis Kurtosis kurtosis-0.516
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0209
Highest regularization parameter α highest_alpha42220000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.713; Stabil: 1.000; Sysdev: 0.000; Positv: 1.000; Valcen: 0.894; Smooth: 0.894

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd5pgma_
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_idd5pgmb_
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_idd5pgmc_
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_idd5pgmd_
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_idd5pgme_
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_idd5pgmf_
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_idd5pgmg_
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_idd5pgmh_
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 (8 domains)

Domain ID domain_id5pgmA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1240 — Phosphoglycerate mutase-like
Domain ID domain_id5pgmB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1240 — Phosphoglycerate mutase-like
Domain ID domain_id5pgmC00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1240 — Phosphoglycerate mutase-like
Domain ID domain_id5pgmD00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1240 — Phosphoglycerate mutase-like
Domain ID domain_id5pgmE00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1240 — Phosphoglycerate mutase-like
Domain ID domain_id5pgmF00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1240 — Phosphoglycerate mutase-like
Domain ID domain_id5pgmG00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1240 — Phosphoglycerate mutase-like
Domain ID domain_id5pgmH00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1240 — Phosphoglycerate mutase-like

8. Citations (3)

9. Files and Curves (10)