4m76

Integrin I domain of complement receptor 3 in complex with C3d

Method: X-RAY DIFFRACTION Dmax: 90.3 Å Quality: GOOD

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

Complement C3

Homo sapiens

UniProt P01024

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 994–1288 Fragment:unp residues 994-1288 Mutation:C1010A, C144A, I332G Integrin alpha-M × 1 (P11215) NI NICKEL (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;PEG 3350, pH 7, vapor diffusion, hanging drop, temperature 298K Resolution 2.80 Å R-free 0.242

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.

74 other PDB entries and 117 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CO3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–298; UniProt 994–1288

Integrin alpha-M

Homo sapiens

UniProt P11215

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 143–337 Fragment:unp residues 143-337 Complement C3 × 1 (P01024) NI NICKEL (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;PEG 3350, pH 7, vapor diffusion, hanging drop, temperature 298K Resolution 2.80 Å R-free 0.242

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.

30 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ITAM_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–198; UniProt 143–337

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 4m76

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4m76
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4m76
Deposition date deposition_date2013-08-12
Structure title titleIntegrin I domain of complement receptor 3 in complex with C3d
Keywords keywords;integrin, complement receptor, immunity, innate immunity, inflammation, phagocytosis, Mac-1, CD11b/CD18, alphaMbeta2, macrophage, Rossmann fold, I domain, Von Willebrand Factor A (VWA), alpha-alpha barrel, adhesion, cell adhesion ;; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.33
Radius of gyration Rg (electron density) rg_electron26.90
Forward intensity I(0) i045364300.00
Molecular weight molecular_weight53541.0 kDa
Excluded volume excluded_volume67555 ų
Envelope volume envelope_volume81297 ų
Hydration-shell volume shell_volume26344 ų
Envelope diameter envelope_diameter97.2
Shell Rg shell_rg32.96
Envelope Rg envelope_rg27.07
Shape Rg shape_rg26.90
Total Rg total_rg27.58
Total atoms total_atoms3771
Residues n_residues475
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 dmax90.3
Rg (real space) rg_real27.51
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real4.5360e+07
I(0) uncertainty (real space) i0_real_error6.9710e+05
Rg (reciprocal space) rg_reciprocal27.46
I(0) (reciprocal space) i0_reciprocal45360000.0000
Solution quality estimate total_estimate0.8670
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.5
Skewness Skewness skewness0.477
Kurtosis Kurtosis kurtosis-0.439
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13190000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.800; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.909; Smooth: 0.956

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd4m76a1
Class classa — All alpha proteins
Fold Fold folda.102 — alpha/alpha toroid
Superfamily Superfamily superfamilya.102.4 — Terpenoid cyclases/Protein prenyltransferases
Family Family familya.102.4.4 — Complement components
Domain ID domain_idd4m76a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4m76b_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.62 — vWA-like
Superfamily Superfamily superfamilyc.62.1 — vWA-like
Family Family familyc.62.1.1 — Integrin A (or I) domain

CATH v4.4 (2 domains)

Domain ID domain_id4m76A00
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily20
Domain ID domain_id4m76B00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily410 — von Willebrand factor, type A domain

8. Citations (1)

9. Files and Curves (10)