8k9r

Cryo EM structure of the products-bound PGAP1(Bst1)-H443N from Chaetomium thermophilum

Method: ELECTRON MICROSCOPY

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

GPI inositol-deacylase,MCherry protein

Psychromonas sp. B3M02

UniProt A0A366VY15

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Heteromer Protein 2 Green fluorescent protein,Complement decay-accelerating factor × 1 (P08174) alpha-D-mannopyranose × 2 2-azanylethyl [(2~{S},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-2,4,5-tris(oxidanyl)oxan-3-yl] hydrogen phosphate × 1 2-amino-2-deoxy-alpha-D-glucopyranose × 1 ;[(2~{R})-1-octadecoxy-3-[oxidanyl-[(2~{R},3~{R},5~{S},6~{R})-2,3,4,5,6-pentakis(oxidanyl)cyclohexyl]oxy-phosphoryl]oxy-propan-2-yl] octadecanoate ; × 1 PALMITIC ACID × 1 CHOLESTEROL × 1 2-azanylethyl [(2R,3S,4S,5S,6S)-3,4,5,6-tetrakis(oxidanyl)oxan-2-yl]methyl hydrogen phosphate × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name A0A366VY15_9GAMM
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1201–1435; UniProt 2–236

GPI inositol-deacylase,MCherry protein

Psychromonas sp. B3M02

UniProt G0S652

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Heteromer Protein 2 Green fluorescent protein,Complement decay-accelerating factor × 1 (P08174) alpha-D-mannopyranose × 2 2-azanylethyl [(2~{S},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-2,4,5-tris(oxidanyl)oxan-3-yl] hydrogen phosphate × 1 2-amino-2-deoxy-alpha-D-glucopyranose × 1 ;[(2~{R})-1-octadecoxy-3-[oxidanyl-[(2~{R},3~{R},5~{S},6~{R})-2,3,4,5,6-pentakis(oxidanyl)cyclohexyl]oxy-phosphoryl]oxy-propan-2-yl] octadecanoate ; × 1 PALMITIC ACID × 1 CHOLESTEROL × 1 2-azanylethyl [(2R,3S,4S,5S,6S)-3,4,5,6-tetrakis(oxidanyl)oxan-2-yl]methyl hydrogen phosphate × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name G0S652_CHATD
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–1186; UniProt 2–1184

Green fluorescent protein,Complement decay-accelerating factor

Homo sapiens

UniProt P08174

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Heteromer Protein 2 GPI inositol-deacylase,MCherry protein × 1 (A0A366VY15,G0S652) alpha-D-mannopyranose × 2 2-azanylethyl [(2~{S},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-2,4,5-tris(oxidanyl)oxan-3-yl] hydrogen phosphate × 1 2-amino-2-deoxy-alpha-D-glucopyranose × 1 ;[(2~{R})-1-octadecoxy-3-[oxidanyl-[(2~{R},3~{R},5~{S},6~{R})-2,3,4,5,6-pentakis(oxidanyl)cyclohexyl]oxy-phosphoryl]oxy-propan-2-yl] octadecanoate ; × 1 PALMITIC ACID × 1 CHOLESTEROL × 1 2-azanylethyl [(2R,3S,4S,5S,6S)-3,4,5,6-tetrakis(oxidanyl)oxan-2-yl]methyl hydrogen phosphate × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name DAF_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 264–272; UniProt 345–353

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.

2. Structure Basics 2. Structure Basics

Entry ID entry_id8k9r
Deposition date deposition_date2023-08-01
Structure title titleCryo EM structure of the products-bound PGAP1(Bst1)-H443N from Chaetomium thermophilum
Keywords keywords;Bst1, Glycosylphosphatidylinositol, GPI anchoring, GPI-AP, GPI-AP remodelase, Integral membrane enzyme, Lipase, Lipid remodeling, Membrane enzyme, Membrane protein, Nanodisc, PGAP1, TGP, Thermostable green fluorescence protein, Transmembrane enzyme, Triad enzyme. ;; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

8k9r__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

8k9r__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

8k9r__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)33.63 Å
Rg (electron density)33.10 Å
Total Rg33.56 Å
Atom count7684
Residues962
Excluded volume138700 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8k9r__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download

4. Crystallography and Experiment 4. Crystallography & Experiment

5. Entities and Polymers Entities & Polymers (9)

7. Citations (1)