7srk

Single chain trimer HLA-A*24:02 (Y108C, A163C) with 8mer peptide YPPVPETF

Method: X-RAY DIFFRACTION Dmax: 103.8 Å Quality: GOOD

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

RPA-related protein RADX peptide,Beta-2-microglobulin,MHC class I antigen chimera

Homo sapiens

UniProt A0A411J078

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 25–299 Mutation:Y108C, A163C VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295 K;100 mM MES, pH 6.0, 200 mM KSCN, 18% Peg 3350 Resolution 2.50 Å R-free 0.260
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 25–299 Mutation:Y108C, A163C VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295 K;100 mM MES, pH 6.0, 200 mM KSCN, 18% Peg 3350 Resolution 2.50 Å R-free 0.260

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.

24 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A411J078_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 143–417; UniProt 25–299 Author chain C; PDBConstruct 143–417; UniProt 25–299

RPA-related protein RADX peptide,Beta-2-microglobulin,MHC class I antigen chimera

Homo sapiens

UniProt P16213

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 21–119 Mutation:Y108C, A163C VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295 K;100 mM MES, pH 6.0, 200 mM KSCN, 18% Peg 3350 Resolution 2.50 Å R-free 0.260
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 21–119 Mutation:Y108C, A163C VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295 K;100 mM MES, pH 6.0, 200 mM KSCN, 18% Peg 3350 Resolution 2.50 Å R-free 0.260

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.

8 other PDB entries and 58 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B2MG_PONPY
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 24–122; UniProt 21–119 Author chain C; PDBConstruct 24–122; UniProt 21–119

RPA-related protein RADX peptide,Beta-2-microglobulin,MHC class I antigen chimera

Homo sapiens

UniProt Q6NSI4

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 509–516 Mutation:Y108C, A163C VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295 K;100 mM MES, pH 6.0, 200 mM KSCN, 18% Peg 3350 Resolution 2.50 Å R-free 0.260
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 509–516 Mutation:Y108C, A163C VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295 K;100 mM MES, pH 6.0, 200 mM KSCN, 18% Peg 3350 Resolution 2.50 Å R-free 0.260

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.

3 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RADX_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–8; UniProt 509–516 Author chain C; PDBConstruct 1–8; UniProt 509–516

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 7srk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7srk
Deposition date deposition_date2021-11-08
Structure title titleSingle chain trimer HLA-A*24:02 (Y108C, A163C) with 8mer peptide YPPVPETF
Keywords keywordsHLA, VHH, HPV, SCT, 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_guinier32.17
Radius of gyration Rg (electron density) rg_electron31.34
Forward intensity I(0) i0198560000.00
Molecular weight molecular_weight107720.0 kDa
Excluded volume excluded_volume132540 ų
Envelope volume envelope_volume174560 ų
Hydration-shell volume shell_volume45808 ų
Envelope diameter envelope_diameter108.6
Shell Rg shell_rg38.82
Envelope Rg envelope_rg31.13
Shape Rg shape_rg31.33
Total Rg total_rg31.98
Total atoms total_atoms7602
Residues n_residues983
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 dmax103.8
Rg (real space) rg_real32.02
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real1.9860e+08
I(0) uncertainty (real space) i0_real_error2.9630e+06
Rg (reciprocal space) rg_reciprocal32.08
I(0) (reciprocal space) i0_reciprocal198600000.0000
Solution quality estimate total_estimate0.8761
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.4
Skewness Skewness skewness0.241
Kurtosis Kurtosis kurtosis-0.196
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24460000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.843; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.867

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7srkB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7srkD01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)