6V2O: HLA-B*57:01 presenting the peptide ASLNLPAVSW

HLA-B*57:01 presenting the peptide ASLNLPAVSW. Determined by X-ray diffraction at 1.27 Å resolution. Released 20 May 2020.

Method: X-ray diffraction
Resolution: 1.27 Å
Organisms: Homo sapiens, synthetic construct
Chains: 3
Atoms: 3,756
Mol. weight: 44.73 kDa
Released: 20 May 2020

Explore 6V2O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6V2O contains 14 α-helices and 30 β-strands across 2 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	57-84	28
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	152-161	10
α-helix	163-174	12
α-helix	176-179	4
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	214-219	6	4
β-strand	222-223	2	4
α-helix	225-227	3
β-strand	229-230	2	3
α-helix	231-233	3
β-strand	234-235	2	3
β-strand	241-250	10	3
α-helix	254-256	3
β-strand	257-262	6	4
β-strand	270-272	3	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

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
MHC class I antigen	A	protein	276	Homo sapiens	U6BR87 (AlphaFold model)
Beta-2-microglobulin	B	protein	100	Homo sapiens	P61769 (AlphaFold model)
Peptide ALA-SER-LEU-ASN-LEU-PRO-ALA-VAL-SER-TRP	C	protein	10	synthetic construct	P35221 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6V2O_1 MHC class I antigen (chains A)
GSHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRMAPRAPWIEQEGPEYW
DGETRNMKASAQTYRENLRIALRYYNQSEAGSHIIQVMYGCDVGPDGRLLRGHDQSAYDG
KDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQLRAYLEGLCVEWLRRYLENGKETLQ
RADPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRT
FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP

Sequence of entity 2 (B), FASTA

>6V2O_2 Beta-2-microglobulin (chains B)
MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD
WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM

Sequence of entity 3 (C), FASTA

>6V2O_3 Peptide ALA-SER-LEU-ASN-LEU-PRO-ALA-VAL-SER-TRP (chains C)
ASLNLPAVSW

Primary citation

The molecular basis of how buried human leukocyte antigen polymorphism modulates natural killer cell function. Saunders, P.M., MacLachlan, B.J., Pymm, P. et al. Proc Natl Acad Sci U S A (2020) 117:11636-11647. DOI 10.1073/pnas.1920570117 · PubMed

Other PDB entries of the same protein (UniProt U6BR87 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7R7Y 1.6 Å, Crystal structure of HLA-B*5701 complex with an HIV-1 Gag-derived epitope QW9 S3T variant
8F7M 1.88 Å, Crystal Structure of HLA-B*57:01-TW10-T242N complex
8F5A 1.95 Å, Crystal Structure of KS1 TCR in complex with HLA-B*57:01-TW10
7R7X 2.1 Å, Crystal structure of HLA-B*5701 complex with an HIV-1 Gag-derived epitope QW9

Browse structure collections

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