3E2H: M67 high-affinity mutant of the 2C TCR

Structure of the m67 high-affinity mutant of the 2C TCR in complex with Ld/QL9. Determined by X-ray diffraction at 3.8 Å resolution. Released 4 Nov 2008.

Method: X-ray diffraction
Resolution: 3.8 Å
Organism: Mus musculus
Chains: 4
Atoms: 3,227
Mol. weight: 45.73 kDa
Released: 4 Nov 2008

Explore 3E2H in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3E2H contains 8 α-helices and 32 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: 6 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	5-10	6	1
β-strand	23-28	6	1
β-strand	31-35	5	1
β-strand	37	1	1
β-strand	46-47	2	1
α-helix	50-52	3
α-helix	57-84	28
β-strand	95-103	9	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	164-172	9

Chain B: 0 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	3-4	2	2
β-strand	9-11	3	3
β-strand	18-20	3	2
β-strand	23-24	2	2
β-strand	32-37	6	3
β-strand	43-49	7	3
β-strand	55-58	4	2
β-strand	62-67	6	2
β-strand	72-77	6	2
β-strand	86-92	7	3
β-strand	105	1	3
β-strand	111-113	3	3

Chain C: 1 helix, 11 β-strands

Element	Residues	Length	Sheet
β-strand	5-7	3	4
β-strand	10-14	5	5
β-strand	19-24	6	4
β-strand	31-37	7	5
β-strand	44-49	6	5
β-strand	56-57	2	5
β-strand	65-68	4	4
β-strand	74-79	6	4
α-helix	84-86	3
β-strand	88-95	8	5
β-strand	107-108	2	5
β-strand	112-117	6	5

Chain Q: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	5-7	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
H-2 class I histocompatibility antigen, L-D alpha chain	A	protein	175	Mus musculus	P01897 (AlphaFold model)
QL9 peptide	Q	protein	9		Q60597 (AlphaFold model)
T-cell receptor alpha chain V region PHDS58	B	protein	109	Mus musculus	P01738 (AlphaFold model)
M67 TCR beta chain	C	protein	110	Mus musculus	A2NTY6 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3E2H_1 H-2 class I histocompatibility antigen, L-D alpha chain (chains A)
GPHSMRYYETATSRRGLGEPRYTSVGYVDDKEFVRFDSDAENPRYEPQVPWMEQEGPEYW
ERITQVAKGQEQWFRVNLRTLLGYYNQSAGGTHTLQRMYGCDVGSDGRLLRGYEQFAYDG
CDYIALNEDLRTWTAADMAAQITRRKWEQAGAAEYYRAYLEGECVEWLHRYLKNG

Sequence of entity 2 (Q), FASTA

>3E2H_2 QL9 PEPTIDE (chains Q)
QLSPFPFDL

Sequence of entity 3 (B), FASTA

>3E2H_3 T-cell receptor alpha chain V region PHDS58 (chains B)
SVTQPDARVTVSEGASLQLRCKYSYSATPYLFWYVQYPRQGPQLLLKYYSGDPVVQGVNG
FEAEFSKSNSSFHLRKASVHRSDSAVYFCAVSLERPYLTFGSGTKVIVL

Sequence of entity 4 (C), FASTA

>3E2H_4 M67 TCR beta chain (chains C)
AAVTQSPRNKVAVTGEKVTLSCNQTNNHNNMYWYRQDTGHELRLIYYSYGAGSTEKGDIP
DGYKASRPSQENFSLTLESATPSQTSVYFCASGGGGTLYFGAGTRLSVLS

Primary citation

Distinct CDR3 Conformations in TCRs Determine the Level of Cross-Reactivity for Diverse Antigens, but Not the Docking Orientation. Jones, L.L., Colf, L.A., Stone, J.D. et al. J Immunol (2008) 181:6255-6264. PubMed

Other PDB entries of the same protein (UniProt P01897 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3V4U 1.64 Å, Structure of a monoclonal antibody complexed with its MHC-I antigen
3UO1 1.64 Å, Structure of a monoclonal antibody complexed with its MHC-I antigen
3V52 1.7 Å, Structure of a monoclonal antibody complexed with its MHC-I antigen
3UYR 1.7 Å, Structure of a monoclonal antibody complexed with its MHC-I antigen
6L9K 1.8 Å, H2-Ld a1a2 complexed with A5 peptide
8D5N 1.8 Å, Crystal structure of Ld-HF10
3VJ6 1.9 Å, Structure of the MHC class Ib molecule Qa-1b
4MS8 1.92 Å, 42F3 TCR pCPB9/H-2Ld Complex
3ERY 1.95 Å, Different thermodynamic binding mechanisms and peptide fine specificities associated…
5VCL 2.05 Å, Structure of the Qdm peptide bound to Qa-1a
3TJH 2.12 Å, 42F3-p3A1/H2-Ld complex
2OI9 2.35 Å, Structure of the 2C/Ld/QL9 allogeneic complex

Browse structure collections

About this viewer

MolViewer shows 3E2H 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.