1H15: HLA-DRA10101/DRB50101

X-ray crystal structure of HLA-DRA1*0101/DRB5*0101 complexed with a peptide from Epstein Barr Virus DNA polymerase. Determined by X-ray diffraction at 3.1 Å resolution. Released 3 Oct 2002.

Method: X-ray diffraction
Resolution: 3.1 Å
Organisms: HOMO SAPIENS, HUMAN HERPESVIRUS 4
Chains: 6
Atoms: 6,420
Mol. weight: 91.12 kDa
Ligands: NAG
Released: 3 Oct 2002

Explore 1H15 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1H15 contains 20 α-helices and 62 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: 3 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	5-15	11	1
β-strand	19-26	8	1
β-strand	29-35	7	1
β-strand	40-43	4	1
α-helix	46-51	6
β-strand	52-53	2	2
α-helix	56-75	20
α-helix	80-82	3
β-strand	85	1	3
β-strand	89-93	5	4
β-strand	103-112	10	4
β-strand	113	1	3
β-strand	117-123	7	5
β-strand	126-128	3	5
β-strand	133-134	2	4
β-strand	138-139	2	4
β-strand	145-153	9	4
β-strand	160-167	8	5
β-strand	174-179	6	5

Chain B: 5 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	7-18	12	1
β-strand	23-32	10	1
β-strand	35-41	7	1
β-strand	47-49	3	1
β-strand	51	1	6
α-helix	55-61	7
α-helix	65-74	10
α-helix	75-80	6
α-helix	81-84	4
α-helix	87-89	3
β-strand	98	1	7
β-strand	101-104	4	7
β-strand	113-122	10	7
β-strand	128-133	6	8
β-strand	137	1	8
β-strand	142-144	3	7
β-strand	148-149	2	7
β-strand	155-163	9	7
β-strand	170-176	7	8
β-strand	184-189	6	8

Chains C and F: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
β-strand	629-630	2	2
α-helix	634-636	3

Chain D: 5 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	5-14	10	9
α-helix	15-17	3
β-strand	19-26	8	9
β-strand	29-35	7	9
β-strand	40-43	4	9
α-helix	46-51	6
β-strand	52-53	2	10
α-helix	56-75	20
α-helix	80-83	4
β-strand	85	1	11
α-helix	86-87	2
β-strand	88-93	6	12
β-strand	103-112	10	12
β-strand	113	1	11
β-strand	120-123	4	13
β-strand	126-127	2	13
β-strand	134	1	12
β-strand	138-139	2	12
β-strand	145-153	9	12
β-strand	161-165	5	13
β-strand	174-178	5	13

Chain E: 5 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	8-18	11	9
β-strand	23-32	10	9
β-strand	35-41	7	9
β-strand	47-49	3	9
β-strand	51	1	6
α-helix	55-61	7
α-helix	67-70	4
α-helix	74	1
α-helix	75-80	6
α-helix	81-84	4
β-strand	98-103	6	14
β-strand	115-120	6	14
β-strand	128-133	6	15
β-strand	136-138	3	15
β-strand	142-144	3	14
β-strand	156-161	6	14
β-strand	170-176	7	15
β-strand	184-189	6	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
HLA class II histocompatibility antigen, dr alpha chain	A, D	protein	182	HOMO SAPIENS	P01903 (AlphaFold model)
HLA class II histocompatibility antigen, dr beta 1 chain	B, E	protein	190	HOMO SAPIENS	Q30154 (AlphaFold model)
DNA polymerase	C, F	protein	14	HUMAN HERPESVIRUS 4	P03198 (AlphaFold model)

Sequence of entity 1 (A, D), FASTA

>1H15_1 HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN (chains A, D)
IKEEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGAL
ANIAVDKANLEIMTKRSNYTPITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVT
WLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDVYDCRVEHWGLDEPLLKHWEF
DA

Sequence of entity 2 (B, E), FASTA

>1H15_2 HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR BETA 1 CHAIN (chains B, E)
GDTRPRFLQQDKYECHFFNGTERVRFLHRDIYNQEEDLRFDSDVGEYRAVTELGRPDAEY
WNSQKDFLEDRRAAVDTYCRHNYGVGESFTVQRRVEPKVTVYPARTQTLQHHNLLVCSVN
GFYPGSIEVRWFRNSQEEKAGVVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSV
TSPLTVEWRA

Sequence of entity 3 (C, F), FASTA

>1H15_3 DNA POLYMERASE (chains C, F)
GGVYHFVKKHVHES

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	3

Primary citation

A Functional and Structural Basis for Tcr Cross-Reactivity in Multiple Sclerosis. Lang, H., Jacobsen, H., Ikemizu, S. et al. Nat Immunol (2002) 3:940. DOI 10.1038/NI835 · PubMed

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

5NI9 1.33 Å, Crystal structure of HLA-DRB1*04:01 with the alpha-enolase peptide 326-340
4X5W 1.34 Å, HLA-DR1 with CLIP102-120(M107W)
5NIG 1.35 Å, Crystal structure of HLA-DRB1*04:01 with modified alpha-enolase peptide 326-340…
8CMC 1.42 Å, Human Leukocyte Antigen class II allotype DR1 presenting SARS-CoV-2 Spike peptide S511-530
8PJF 1.48 Å, Human Leukocyte Antigen class II allotype DR1 presenting P11T->R modified influenza A…
6QZC 1.64 Å, HLA-DR1 with the QAR Peptide
8CMG 1.64 Å, Human Leukocyte Antigen class II allotype DR1 presenting SARS-CoV-2 nsp14 peptide…
8CMH 1.64 Å, Human Leukocyte Antigen class II allotype DR1 presenting SARS-CoV-2 Omicron (BA.1) Spike…
4MD5 1.65 Å, Immune Receptor
4MDJ 1.7 Å, Immune Receptor
8PJE 1.7 Å, Human Leukocyte Antigen class II allotype DR1 presenting influenza A virus…
7YX9 1.76 Å, MHC-II dynamics are maintained in HLA-DR allotypes to ensure catalyzed peptide exchange

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1H15: HLA-DRA1*0101/DRB5*0101