7ysg

Cryo-EM structure of human FcmR bound to sIgM

Method: ELECTRON MICROSCOPY Dmax: 177.1 Å Quality: GOOD

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

Immunoglobulin heavy constant mu

Homo sapiens

UniProt P01871

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 × 16 其他Polymer 1 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain A; UniProt 222–453 Chain B; UniProt 222–453 Chain C; UniProt 222–453 Chain D; UniProt 222–453 Chain E; UniProt 222–453 Chain F; UniProt 222–453 Chain G; UniProt 222–453 Chain H; UniProt 222–453 Chain K; UniProt 222–453 Chain L; UniProt 222–453 Not recorded Immunoglobulin J chain × 1 (P01591) Secretory component × 1 (P01833) Fas apoptotic inhibitory molecule 3 × 4 (O60667) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGHM_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–232; UniProt 222–453 Author chain B; PDBConstruct 1–232; UniProt 222–453 Author chain C; PDBConstruct 1–232; UniProt 222–453 Author chain D; PDBConstruct 1–232; UniProt 222–453 Author chain E; PDBConstruct 1–232; UniProt 222–453 Author chain F; PDBConstruct 1–232; UniProt 222–453 Author chain G; PDBConstruct 1–232; UniProt 222–453 Author chain H; PDBConstruct 1–232; UniProt 222–453 Author chain K; PDBConstruct 1–232; UniProt 222–453 Author chain L; PDBConstruct 1–232; UniProt 222–453

Immunoglobulin J chain

Homo sapiens

UniProt P01591

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 × 16 其他Polymer 1 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain J; UniProt 24–159 Not recorded Immunoglobulin heavy constant mu × 10 (P01871) Secretory component × 1 (P01833) Fas apoptotic inhibitory molecule 3 × 4 (O60667) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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.

23 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGJ_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain J; PDBConstruct 1–136; UniProt 24–159

Secretory component

Homo sapiens

UniProt P01833

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 × 16 其他Polymer 1 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain P; UniProt 19–559 Not recorded Immunoglobulin heavy constant mu × 10 (P01871) Immunoglobulin J chain × 1 (P01591) Fas apoptotic inhibitory molecule 3 × 4 (O60667) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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.

15 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PIGR_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain P; PDBConstruct 1–541; UniProt 19–559

Fas apoptotic inhibitory molecule 3

Homo sapiens

UniProt O60667

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 × 16 其他Polymer 1 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain R; UniProt 18–124 Chain S; UniProt 18–124 Chain U; UniProt 18–124 Chain V; UniProt 18–124 Not recorded Immunoglobulin heavy constant mu × 10 (P01871) Immunoglobulin J chain × 1 (P01591) Secretory component × 1 (P01833) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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.

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

View Construct and Data Evidence
UniProt name FAIM3_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain R; PDBConstruct 1–107; UniProt 18–124 Author chain S; PDBConstruct 1–107; UniProt 18–124 Author chain U; PDBConstruct 1–107; UniProt 18–124 Author chain V; PDBConstruct 1–107; UniProt 18–124

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 7ysg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ysg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7ysg
Deposition date deposition_date2022-08-12
Structure title titleCryo-EM structure of human FcmR bound to sIgM
Keywords keywordsimmunoglobin M, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.76
Radius of gyration Rg (electron density) rg_electron55.58
Forward intensity I(0) i01940210000.00
Molecular weight molecular_weight365460.0 kDa
Excluded volume excluded_volume456020 ų
Envelope volume envelope_volume710480 ų
Hydration-shell volume shell_volume105210 ų
Envelope diameter envelope_diameter189.0
Shell Rg shell_rg59.01
Envelope Rg envelope_rg54.99
Shape Rg shape_rg55.61
Total Rg total_rg55.55
Total atoms total_atoms25676
Residues n_residues3290
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 dmax177.1
Rg (real space) rg_real55.68
Rg uncertainty (real space) rg_real_error1.55
I(0) (real space) i0_real1.9400e+09
I(0) uncertainty (real space) i0_real_error3.6830e+07
Rg (reciprocal space) rg_reciprocal55.82
I(0) (reciprocal space) i0_reciprocal1941000000.0000
Solution quality estimate total_estimate0.8567
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.2
Skewness Skewness skewness0.266
Kurtosis Kurtosis kurtosis-0.407
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha163800000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.935; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.344

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 19 domains

CATH v4.4 (19 domains)

Domain ID domain_id7ysgA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7ysgA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7ysgB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7ysgC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7ysgC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7ysgD01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7ysgD02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7ysgE01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7ysgE02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7ysgF01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7ysgG01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7ysgG02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7ysgH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7ysgH02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7ysgK01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7ysgK02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7ysgL01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7ysgR01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7ysgV01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)