6O9B: HLA-A3*01

Crystal structure of HLA-A3*01 in complex with a wild-type beta-catenin peptide. Determined by X-ray diffraction at 2.2 Å resolution. Released 13 Nov 2019.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 3
Atoms: 3,469
Mol. weight: 51.16 kDa
Released: 13 Nov 2019

Explore 6O9B in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6O9B contains 11 α-helices and 30 β-strands across 3 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: 8 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	3-14	12	1
β-strand	18-28	11	1
β-strand	31-37	7	1
β-strand	46-47	2	1
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	152-158	7
α-helix	159-163	5
α-helix	164-174	11
α-helix	176-179	4
β-strand	183	1	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
β-strand	228-230	3	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	270-273	4	4

Chain B: 2 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	23	1	5
α-helix	24-25	2
β-strand	26-31	6	6
β-strand	41-50	10	6
β-strand	51	1	5
β-strand	56-61	6	7
β-strand	64-65	2	7
α-helix	66	1
β-strand	70-71	2	6
β-strand	75-76	2	6
β-strand	82-90	9	6
β-strand	98-103	6	7
β-strand	111-114	4	7

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	2-8	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
HLA class I histocompatibility antigen, A-3 alpha chain	A	protein	300	Homo sapiens	P04439 (AlphaFold model)
Beta-2-microglobulin	B	protein	119	Homo sapiens	P61769 (AlphaFold model)
Catenin beta-1	C	protein	9	Homo sapiens	P35222 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6O9B_1 HLA class I histocompatibility antigen, A-3 alpha chain (chains A)
MASGSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGP
EYWDQETRNVKAQSQTDRVDLGTLRGYYNQSEAGSHTIQIMYGCDVGSDGRFLRGYRQDA
YDGKDYIALNEDLRSWTAADMAAQITKRKWEAAHEAEQLRAYLDGTCVEWLRRYLENGKE
TLQRTDPPKTHMTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAG
DGTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWELSSQPGSLHHILDAQKMVWNHR

Sequence of entity 2 (B), FASTA

>6O9B_2 Beta-2-microglobulin (chains B)
MSRSVALAVLALLSLSGLEAIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLL
KNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM

Sequence of entity 3 (C), FASTA

>6O9B_3 Catenin beta-1 (chains C)
TTAPSLSGK

Primary citation

An engineered antibody fragment targeting mutant beta-catenin via major histocompatibility complex I neoantigen presentation. Miller, M.S., Douglass, J., Hwang, M.S. et al. J Biol Chem (2019) 294:19322-19334. DOI 10.1074/jbc.RA119.010251 · PubMed

Other PDB entries of the same protein (UniProt P04439 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3MRE 1.1 Å, Crystal Structure of MHC class I HLA-A2 molecule complexed with EBV bmlf1-280-288…
3D25 1.3 Å, Crystal structure of HA-1 minor histocompatibility antigen bound to human class I MHC…
3MRG 1.3 Å, Crystal Structure of MHC class I HLA-A2 molecule complexed with HCV NS3-1073-1081…
6JOZ 1.35 Å, Crystal structure of BRLF peptide from EBV in complex with HLA-A1101.
5C0G 1.37 Å, HLA-A02 carrying YLGGPDFPTI
5N1Y 1.39 Å, HLA-A02 carrying MVWGPDPLYV
1I4F 1.4 Å, Crystal structure of HLA-A*0201/MAGE-A4-peptide complex
1OGA 1.4 Å, A structural basis for immunodominant human T-cell receptor recognition.
3MRB 1.4 Å, Crystal Structure of MHC class I HLA-A2 molecule complexed with HCMV pp65-495-503…
3MRK 1.4 Å, Crystal Structure of MHC class I HLA-A2 molecule complexed with AFP137 nonapeptide
6J2A 1.4 Å, The structure of HLA-A*3003/NP44
1X7Q 1.45 Å, Crystal structure of HLA-A*1101 with sars nucleocapsid peptide

Browse structure collections

About this viewer

MolViewer shows 6O9B directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.