1p4l

Crystal structure of NK receptor Ly49C mutant with its MHC class I ligand H-2Kb

Method: X-RAY DIFFRACTION Dmax: 74.7 Å Quality: EXCELLENT

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

MHC CLASS I H-2KB HEAVY CHAIN

Mus musculus

UniProt P01901

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 22–295 Fragment:extracellular alpha-1, alpha-2, alpha-3 Beta-2-microglobulin × 2 (P01887) Ovalbumin peptide × 2 (P01012) LY49-C × 2 (Q64329) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;Protein 8mg/ml, 0.1 M HEPES-Na pH 7.5, 2% v/v PEG400, 2.0 M Ammonium Sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.90 Å R-free 0.295

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.

83 other PDB entries and 140 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HA1B_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–274; UniProt 22–295

Beta-2-microglobulin

Mus musculus

UniProt P01887

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 21–119 Not recorded MHC CLASS I H-2KB HEAVY CHAIN × 2 (P01901) Ovalbumin peptide × 2 (P01012) LY49-C × 2 (Q64329) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;Protein 8mg/ml, 0.1 M HEPES-Na pH 7.5, 2% v/v PEG400, 2.0 M Ammonium Sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.90 Å R-free 0.295

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.

290 other PDB entries and 483 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B2MG_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–99; UniProt 21–119

Ovalbumin peptide

OrganismNot specified

UniProt P01012

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain P; UniProt 257–264 Not recorded MHC CLASS I H-2KB HEAVY CHAIN × 2 (P01901) Beta-2-microglobulin × 2 (P01887) LY49-C × 2 (Q64329) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;Protein 8mg/ml, 0.1 M HEPES-Na pH 7.5, 2% v/v PEG400, 2.0 M Ammonium Sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.90 Å R-free 0.295

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.

10 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name OVAL_CHICK
Isoform
PDB entities 3
Chains and sequence ranges Author chain P; PDBConstruct 1–8; UniProt 257–264

LY49-C

Mus musculus

UniProt Q64329

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain D; UniProt 142–263 Fragment:C-Type Lectin-Like Domain Mutation:S171G, E193G, R223K MHC CLASS I H-2KB HEAVY CHAIN × 2 (P01901) Beta-2-microglobulin × 2 (P01887) Ovalbumin peptide × 2 (P01012) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;Protein 8mg/ml, 0.1 M HEPES-Na pH 7.5, 2% v/v PEG400, 2.0 M Ammonium Sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.90 Å R-free 0.295

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.

2 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KLRA3_MOUSE
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–122; UniProt 142–263

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 1p4l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1p4l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1p4l
Deposition date deposition_date2003-04-23
Structure title titleCrystal structure of NK receptor Ly49C mutant with its MHC class I ligand H-2Kb
Keywords keywordsNatural Killer Receptor, MHC class I, C-type Lectin-like domain, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.71
Radius of gyration Rg (electron density) rg_electron23.59
Forward intensity I(0) i057112000.00
Molecular weight molecular_weight58692.0 kDa
Excluded volume excluded_volume73347 ų
Envelope volume envelope_volume88544 ų
Hydration-shell volume shell_volume30538 ų
Envelope diameter envelope_diameter76.7
Shell Rg shell_rg31.40
Envelope Rg envelope_rg23.60
Shape Rg shape_rg23.58
Total Rg total_rg24.50
Total atoms total_atoms4134
Residues n_residues502
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 dmax74.7
Rg (real space) rg_real24.53
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real5.7110e+07
I(0) uncertainty (real space) i0_real_error6.8820e+05
Rg (reciprocal space) rg_reciprocal24.57
I(0) (reciprocal space) i0_reciprocal57110000.0000
Solution quality estimate total_estimate0.9074
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.0
Skewness Skewness skewness0.131
Kurtosis Kurtosis kurtosis-0.449
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12410000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.936; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1p4la1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)
Domain ID domain_idd1p4la2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.19 — MHC antigen-recognition domain
Superfamily Superfamily superfamilyd.19.1 — MHC antigen-recognition domain
Family Family familyd.19.1.1 — MHC antigen-recognition domain
Domain ID domain_idd1p4lb_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)
Domain ID domain_idd1p4ld_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.169 — C-type lectin-like
Superfamily Superfamily superfamilyd.169.1 — C-type lectin-like
Family Family familyd.169.1.1 — C-type lectin domain

CATH v4.4 (4 domains)

Domain ID domain_id1p4lA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology500 — Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1
Homologous superfamily homologous superfamily10 — MHC class I-like antigen recognition-like
Domain ID domain_id1p4lA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1p4lB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1p4lD00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology100 — Mannose-Binding Protein A; Chain A
Homologous superfamily homologous superfamily10 — Mannose-Binding Protein A, subunit A

8. Citations (1)

9. Files and Curves (10)