8i91

ACE2-SIT1 complex bound with proline

Method: ELECTRON MICROSCOPY Dmax: 180.0 Å Quality: GOOD

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

Angiotensin-converting enzyme 2

Homo sapiens

UniProt Q9BYF1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 14 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 2–805 Chain C; UniProt 2–805 Not recorded SIT1 × 2 (Q9NP91) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 14 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ZN ZINC ION × 2 PRO PROLINE × 2 CL CHLORIDE ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 Å

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.

338 other PDB entries and 388 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACE2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–814; UniProt 2–805 Author chain C; PDBConstruct 3–814; UniProt 2–805

SIT1

Homo sapiens

UniProt Q9NP91

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 14 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–592 Chain D; UniProt 1–592 Not recorded Angiotensin-converting enzyme 2 × 2 (Q9BYF1) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 14 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ZN ZINC ION × 2 PRO PROLINE × 2 CL CHLORIDE ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 Å

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.

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

View Construct and Data Evidence
UniProt name S6A20_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 22–613; UniProt 1–592 Author chain D; PDBConstruct 22–613; UniProt 1–592

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 8i91

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8i91
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8i91
Deposition date deposition_date2023-02-06
Structure title titleACE2-SIT1 complex bound with proline
Keywords keywordstransporter, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier59.54
Radius of gyration Rg (electron density) rg_electron59.88
Forward intensity I(0) i01249510000.00
Molecular weight molecular_weight308860.0 kDa
Excluded volume excluded_volume390890 ų
Envelope volume envelope_volume584350 ų
Hydration-shell volume shell_volume84441 ų
Envelope diameter envelope_diameter198.9
Shell Rg shell_rg57.06
Envelope Rg envelope_rg58.53
Shape Rg shape_rg59.83
Total Rg total_rg59.95
Total atoms total_atoms21764
Residues n_residues2656
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 dmax180.0
Rg (real space) rg_real59.65
Rg uncertainty (real space) rg_real_error2.09
I(0) (real space) i0_real1.2500e+09
I(0) uncertainty (real space) i0_real_error2.7960e+07
Rg (reciprocal space) rg_reciprocal59.40
I(0) (reciprocal space) i0_reciprocal1249000000.0000
Solution quality estimate total_estimate0.8399
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary76.2
Skewness Skewness skewness0.259
Kurtosis Kurtosis kurtosis-0.639
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha61650000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.976; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.001

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)