5JLZ: HLA-DRB1*04:01

Crystal structure of HLA-DRB1*04:01 in complex with modified alpha-enolase peptide 26-40 with citrulline at the position 32. Determined by X-ray diffraction at 1.99 Å resolution. Released 7 Dec 2016.

Method
X-ray diffraction
Resolution
1.99 Å
Organism
Homo sapiens
Chains
6
Atoms
6,705
Mol. weight
93.03 kDa
Ligands
MLA
Released
7 Dec 2016

Explore 5JLZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5JLZ contains 30 α-helices and 64 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 6 helices, 16 β-strands

ElementResiduesLengthSheet
β-strand5-15111
β-strand19-2681
β-strand29-3571
β-strand40-4341
α-helix48-514
β-strand52-5322
α-helix56-7621
α-helix80-845
β-strand8513
α-helix86-872
β-strand88-9364
β-strand103-112104
β-strand11313
β-strand118-12365
β-strand126-12835
β-strand133-13424
α-helix1371
β-strand138-13924
β-strand145-15394
β-strand160-16675
α-helix1731
β-strand174-17965
Chains B and D: 7 helices, 15 β-strands
ElementResiduesLengthSheet
β-strand7-18121
β-strand23-32101
β-strand35-4171
β-strand47-4931
α-helix52-543
α-helix55-628
α-helix65-728
α-helix741
α-helix75-806
α-helix81-866
α-helix87-893
β-strand9516
β-strand98-10367
β-strand113-122107
β-strand12316
β-strand128-13368
β-strand136-13838
β-strand142-14437
β-strand148-14927
β-strand155-16397
β-strand170-17678
β-strand184-18968
Chain C: 6 helices, 16 β-strands
ElementResiduesLengthSheet
β-strand5-15119
β-strand19-2689
β-strand29-3579
β-strand40-4349
α-helix48-514
β-strand52-53210
α-helix56-7621
α-helix80-845
β-strand85111
α-helix86-872
β-strand88-93612
β-strand103-1121012
β-strand113111
β-strand118-123613
β-strand126-127213
β-strand133-134212
α-helix1371
β-strand138-139212
β-strand145-153912
β-strand161-166613
α-helix1731
β-strand174-178513
Chains E and F: 2 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand29-3022
α-helix31-344
α-helix36-394

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
HLA class II histocompatibility antigen, DR alpha chainA, Cprotein189Homo sapiensP01903 (AlphaFold model)
HLA class II histocompatibility antigen, DRB1-4 beta chainB, Dprotein198Homo sapiensP01911 (AlphaFold model)
Alpha-enolaseE, Fprotein15Homo sapiensP06733 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>5JLZ_1 HLA class II histocompatibility antigen, DR alpha chain (chains A, C)
IKEEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGAL
ANIAVDKANLEIMTKRSNYTPITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVT
WLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDVYDCRVEHWGLDEPLLKHWEF
DSSADLVPR
Sequence of entity 2 (B, D), FASTA
>5JLZ_2 HLA class II histocompatibility antigen, DRB1-4 beta chain (chains B, D)
GDTRPRFLEQVKHECHFFNGTERVRFLDRYFYHQEEYVRFDSDVGEYRAVTELGRPDAEY
WNSQKDLLEQKRAAVDTYCRHNYGVGESFTVQRRVYPEVTVYPAKTQPLQHHNLLVCSVN
GFYPGSIEVRWFRNGQEEKTGVVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSL
TSPLTVEWRASSADLVPR
Sequence of entity 3 (E, F), FASTA
>5JLZ_3 Alpha-enolase (chains E, F)
TSKGLFRAAVPSGAS

Ligands and cofactors

IDNameFormulaCopies
MLAMalonic acidC3 H4 O41

Primary citation

Functional and Structural Characterization of a Novel HLA-DRB1*04:01-Restricted alpha-Enolase T Cell Epitope in Rheumatoid Arthritis. Gerstner, C., Dubnovitsky, A., Sandin, C. et al. Front Immunol (2016) 7:494-494. DOI 10.3389/fimmu.2016.00494 · PubMed

Other PDB entries of the same protein (UniProt P01903 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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