Crystal structure of HLA-DR4 presenting citrullinated Tenascin C peptide
Dao, H.D., Loh, T.J., Lim, J.J., Rossjohn, J.To be published.
Experimental Data Snapshot
Starting Model: experimental
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Entity ID: 1 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
HLA class II histocompatibility antigen, DR alpha chain | 189 | Homo sapiens | Mutation(s): 0  Gene Names: HLA-DRA, HLA-DRA1 | ![]() | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P01903 (Homo sapiens) Explore P01903  Go to UniProtKB:  P01903 | |||||
PHAROS:  P01903 GTEx:  ENSG00000204287  | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P01903 | ||||
Glycosylation | |||||
Glycosylation Sites: 1 | Go to GlyGen: P01903-1 | ||||
Sequence AnnotationsExpand | |||||
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Entity ID: 2 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
HLA class II histocompatibility antigen DR beta chain | 198 | Homo sapiens | Mutation(s): 0  Gene Names: HLA-DRB1 | ![]() | |
UniProt | |||||
Find proteins for A0A1V1IGJ9 (Homo sapiens) Explore A0A1V1IGJ9  Go to UniProtKB:  A0A1V1IGJ9 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | A0A1V1IGJ9 | ||||
Glycosylation | |||||
Glycosylation Sites: 1 | |||||
Sequence AnnotationsExpand | |||||
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Find similar proteins by: Sequence | 3D Structure
Entity ID: 3 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
Tenascin | 14 | Homo sapiens | Mutation(s): 0  | ![]() | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P24821 (Homo sapiens) Explore P24821  Go to UniProtKB:  P24821 | |||||
PHAROS:  P24821 GTEx:  ENSG00000041982  | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P24821 | ||||
Sequence AnnotationsExpand | |||||
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Ligands 2 Unique | |||||
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ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
NAG Query on NAG | D [auth A], F [auth B] | 2-acetamido-2-deoxy-beta-D-glucopyranose C8 H15 N O6 OVRNDRQMDRJTHS-FMDGEEDCSA-N | |||
GOL Query on GOL | E [auth A], G [auth B], H [auth B] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |
Modified Residues 1 Unique | |||||
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ID | Chains | Type | Formula | 2D Diagram | Parent |
CIR Query on CIR | C | L-PEPTIDE LINKING | C6 H13 N3 O3 | ARG |
Length ( Å ) | Angle ( ˚ ) |
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a = 119.3 | α = 90 |
b = 119.3 | β = 90 |
c = 73.273 | γ = 120 |
Software Name | Purpose |
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PHENIX | refinement |
XDS | data reduction |
Aimless | data scaling |
PHASER | phasing |
Funding Organization | Location | Grant Number |
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Not funded | -- |