8ISN: HLA-A24

HLA-A24 in complex with modified 9mer WT1 peptide. Determined by X-ray diffraction at 2.48 Å resolution. Released 13 Sept 2023.

Method: X-ray diffraction
Resolution: 2.48 Å
Organism: Homo sapiens
Chains: 6
Atoms: 6,495
Mol. weight: 96.85 kDa
Released: 13 Sept 2023

Explore 8ISN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8ISN contains 28 α-helices and 63 β-strands across 4 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: 11 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	3-12	10	1
α-helix	20	1
β-strand	21-28	8	1
β-strand	31-37	7	1
β-strand	46-47	2	1
α-helix	50-52	3
α-helix	57-85	29
β-strand	94-103	10	1
β-strand	109-118	10	1
β-strand	121-126	6	1
β-strand	133-135	3	1
α-helix	138-149	12
α-helix	152-158	7
α-helix	159-164	6
α-helix	165-174	10
α-helix	176-179	4
α-helix	182	1
β-strand	183	1	2
α-helix	184-185	2
β-strand	186-193	8	3
β-strand	198-208	11	3
β-strand	209	1	2
β-strand	213-219	7	4
β-strand	222-223	2	4
β-strand	228-230	3	3
α-helix	231-233	3
β-strand	234-235	2	3
β-strand	241-250	10	3
β-strand	257-263	7	4
β-strand	270-273	4	4

Chain B: 3 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	5
α-helix	4-5	2
β-strand	6-11	6	6
β-strand	21-30	10	6
β-strand	31	1	5
β-strand	36-41	6	7
β-strand	44-45	2	7
α-helix	46	1
β-strand	50-51	2	6
α-helix	52-54	3
β-strand	55-56	2	6
β-strand	62-70	9	6
β-strand	78-83	6	7
β-strand	91-94	4	7

Chain D: 10 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	3-12	10	8
α-helix	20	1
β-strand	21-28	8	8
β-strand	31-37	7	8
β-strand	46-47	2	8
α-helix	50-52	3
α-helix	57-85	29
β-strand	94-103	10	8
β-strand	109-118	10	8
β-strand	121-126	6	8
β-strand	133-135	3	8
α-helix	138-149	12
α-helix	152-158	7
α-helix	159-163	5
α-helix	164-174	11
β-strand	183	1	9
α-helix	184-185	2
β-strand	186-193	8	10
β-strand	198-208	11	10
β-strand	209	1	9
β-strand	213-219	7	11
β-strand	228-230	3	10
α-helix	231-233	3
β-strand	234-235	2	10
β-strand	241-250	10	10
α-helix	253-256	4
β-strand	257-263	7	11
β-strand	270-272	3	11

Chain E: 4 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	12
α-helix	4-5	2
β-strand	6	1	13
β-strand	9-11	3	14
α-helix	14-15	2
β-strand	21-25	5	14
β-strand	26-30	5	13
β-strand	31	1	12
β-strand	35-41	7	15
β-strand	44-45	2	15
α-helix	46	1
β-strand	50-51	2	16
α-helix	52-54	3
β-strand	55-56	2	13
β-strand	62-65	4	13
β-strand	66-67	2	16
β-strand	68-70	3	14
β-strand	78-84	7	15
β-strand	91-94	4	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
MHC class I antigen	A, D	protein	305	Homo sapiens	D9UAY1 (AlphaFold model)
Beta-2-microglobulin	B, E	protein	99	Homo sapiens	P61769 (AlphaFold model)
Cys-tyr-thr-trp-asn-gln-met-asn-leu	C, F	protein	9	Homo sapiens	P19544 (AlphaFold model)

Sequence of entity 1 (A, D), FASTA

>8ISN_1 MHC class I antigen (chains A, D)
GSHSMRYFSTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYW
DEETGKVKAHSQTDRENLRIALRYYNQSEAGSHTLQMMFGCDVGSDGRFLRGYHQYAYDG
KDYIALKEDLRSWTAADMAAQITKRKWEAAHVAEQQRAYLEGTCVDGLRRYLENGKETLQ
RTDPPKTHMTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT
FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEPGASGDYKDDDDKGGGGLNDIFEAQ
KIEWH

Sequence of entity 2 (B, E), FASTA

>8ISN_2 Beta-2-microglobulin (chains B, E)
IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDW
SFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM

Sequence of entity 3 (C, F), FASTA

>8ISN_3 CYS-TYR-THR-TRP-ASN-GLN-MET-ASN-LEU (chains C, F)
CYTWNQMNL

Primary citation

Elucidation of binding mechanism, affinity, and complex structure between mWT1 tumor-associated antigen peptide and HLA-A*24:02. Bekker, G.J., Numoto, N., Kawasaki, M. et al. Protein Sci (2023) 32:e4775-e4775. DOI 10.1002/pro.4775 · PubMed

Other PDB entries of the same protein (UniProt D9UAY1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7F4W 2.9 Å, Complex structure of HLA2402 with recognizing SARS-CoV-2 epitope pep4

Browse structure collections

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