22wm

Phosphoglycerate mutase 1 complexed with a fragment

Method: X-RAY DIFFRACTION Dmax: 87.5 Å Quality: REASONABLE

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

Phosphoglycerate mutase 1

Homo sapiens

UniProt P18669

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 B; UniProt 1–254 Chain C; UniProt 1–254 Not recorded A1E4R 4-(4-chlorophenyl)benzoic acid × 2 GOL GLYCEROL × 10 CL CHLORIDE ION × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;289.15 K;1 mM MES 6.0, 8% PEG3350 Resolution 1.91 Å R-free 0.229

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.

32 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PGAM1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–254; UniProt 1–254 Author chain C; PDBConstruct 1–254; UniProt 1–254

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 22wm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 22wm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id22wm
Deposition date deposition_date2026-01-26
最后修订 last_revision2026-02-11
Structure title titlePhosphoglycerate mutase 1 complexed with a fragment
Keywords keywordsPGAM1, ISOMERASE, Inhibitor; ISOMERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.38
Radius of gyration Rg (electron density) rg_electron24.73
Forward intensity I(0) i097041700.00
Molecular weight molecular_weight52165.0 kDa
Excluded volume excluded_volume50817 ų
Envelope volume envelope_volume83602 ų
Hydration-shell volume shell_volume28283 ų
Envelope diameter envelope_diameter90.3
Shell Rg shell_rg32.06
Envelope Rg envelope_rg25.07
Shape Rg shape_rg24.66
Total Rg total_rg25.43
Total atoms total_atoms4055
Residues n_residues477
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 dmax87.5
Rg (real space) rg_real25.40
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real9.7040e+07
I(0) uncertainty (real space) i0_real_error1.4910e+06
Rg (reciprocal space) rg_reciprocal25.40
I(0) (reciprocal space) i0_reciprocal97040000.0000
Solution quality estimate total_estimate0.6634
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.8
Skewness Skewness skewness0.423
Kurtosis Kurtosis kurtosis-0.215
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18490000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.782; Stabil: 1.000; Sysdev: 0.120; Positv: 1.000; Valcen: 0.924; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)