2FZ3: PDB entry 2FZ3

The role of T cell receptor alpha genes in directing human MHC restriction. Determined by X-ray diffraction at 1.9 Å resolution. Released 26 Dec 2006.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 3
Atoms: 3,376
Mol. weight: 45.06 kDa
Released: 26 Dec 2006

Explore 2FZ3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2FZ3 contains 15 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: 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	140-149	10
α-helix	152-161	10
α-helix	163-174	12
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	214-219	6	4
β-strand	222-223	2	4
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	35-41	7	7
β-strand	44-45	2	7
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	78-84	7	7
α-helix	90	1
β-strand	91-94	4	7

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	2-4	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
HLA class I histocompatibility antigen, B-35 alpha chain	A	protein	276	Homo sapiens	O19626 (AlphaFold model)
Beta-2-microglobulin	B	protein	99	Homo sapiens	P61769 (AlphaFold model)
11-mer peptide from Epstein-Barr nuclear antigen 1	C	protein	11		P03211 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2FZ3_1 HLA class I histocompatibility antigen, B-35 alpha chain (chains A)
GSHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRTEPRAPWIEQEGPEYW
DRNTQIFKTNTQTYRESLRNLRGYYNQSEAGSHIIQRMYGCDLGPDGRLLRGHDQSAYDG
KDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQRRAYLEGLCVEWLRRYLENGKETLQ
RADPPKTHVTHHPVSDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRT
FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP

Sequence of entity 2 (B), FASTA

>2FZ3_2 Beta-2-microglobulin (chains B)
IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDW
SFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM

Sequence of entity 3 (C), FASTA

>2FZ3_3 11-mer peptide from Epstein-Barr nuclear antigen 1 (chains C)
HPVGEADYFEY

Primary citation

TCR alpha genes direct MHC restriction in the potent human T cell response to a class I-bound viral epitope. Miles, J.J., Borg, N.A., Brennan, R.M. et al. J Immunol (2006) 177:6804-6814. DOI 10.4049/jimmunol.177.10.6804 · PubMed

Other PDB entries of the same protein (UniProt O19626 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2FYY 1.5 Å, The role of T cell receptor alpha genes in directing human MHC restriction
2CIK 1.75 Å, Insights Into Crossreactivity in Human Allorecognition: The Structure of HLA-B35011…
8V51 2.1 Å, Crystal structure of a HLA-B*35:01-NP10 with D1 TCR
8V50 2.65 Å, Crystal structure of a HLA-B*35:01-NP6 with D1 TCR

Browse structure collections

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