3QEU: TCR DMF5

The crystal structure of TCR DMF5. Determined by X-ray diffraction at 2.09 Å resolution. Released 6 Jul 2011.

Method: X-ray diffraction
Resolution: 2.09 Å
Organism: Homo sapiens
Chains: 4
Atoms: 7,373
Mol. weight: 98.92 kDa
Ligands: LI
Released: 6 Jul 2011

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

Secondary structure: helices and β-sheets

3QEU contains 26 α-helices and 88 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: 4 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	3-4	2	11
β-strand	10-13	4	12
α-helix	17	1
β-strand	18-24	7	11
β-strand	31-37	7	12
β-strand	44-49	6	12
β-strand	53-57	5	11
β-strand	60-65	6	11
β-strand	70-75	6	11
α-helix	80-82	3
β-strand	84-91	8	12
β-strand	97-99	3	12
β-strand	103-108	6	12
α-helix	109	1
β-strand	117-121	5	13
β-strand	122-123	2	14
β-strand	131-135	5	13
β-strand	153	1	13
α-helix	154-156	3
β-strand	157-161	5	13
β-strand	166-173	8	13
β-strand	196	1	13

Chain B: 7 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	7-10	4	15
β-strand	13-17	5	16
β-strand	22-24	3	17
β-strand	25-28	4	15
β-strand	34-41	8	16
β-strand	45-52	8	16
β-strand	59-60	2	16
β-strand	67-69	3	17
β-strand	76	1	15
β-strand	79-81	3	17
α-helix	86-88	3
β-strand	90-97	8	16
β-strand	105-106	2	16
β-strand	110-115	6	16
α-helix	118-120	3
β-strand	122	1	18
α-helix	123-124	2
β-strand	125-130	6	14
α-helix	131-132	2
α-helix	133-139	7
β-strand	141-151	11	14
β-strand	152	1	18
β-strand	156-162	7	19
β-strand	165-167	3	19
β-strand	171-173	3	14
α-helix	177	1
β-strand	178-179	2	14
β-strand	189-198	10	14
α-helix	199-202	4
β-strand	209-215	7	19
β-strand	218	1	20
β-strand	232	1	20
β-strand	234-240	7	19

Chain D: 8 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	3-4	2	1
β-strand	10-13	4	2
α-helix	17	1
β-strand	18-24	7	1
β-strand	29-37	9	2
β-strand	44-49	6	2
β-strand	53-57	5	1
β-strand	60-65	6	1
β-strand	70-75	6	1
α-helix	80-82	3
β-strand	84-92	9	2
β-strand	97-99	3	2
β-strand	103-108	6	2
β-strand	117-122	6	3
β-strand	123	1	4
β-strand	130-135	6	3
α-helix	144-146	3
β-strand	151-153	3	3
α-helix	154-156	3
β-strand	157-161	5	3
α-helix	162-164	3
β-strand	166-175	10	3
α-helix	182-185	4
α-helix	192	1
β-strand	196	1	3
α-helix	198-200	3

Chain E: 7 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	7-10	4	5
β-strand	13-17	5	6
β-strand	22-24	3	7
β-strand	25-28	4	5
β-strand	34-41	8	6
β-strand	45-54	10	6
β-strand	57-60	4	6
β-strand	67-69	3	7
β-strand	76	1	5
β-strand	79-81	3	7
α-helix	86-88	3
β-strand	90-97	8	6
β-strand	105-106	2	6
β-strand	110-115	6	6
α-helix	118-120	3
β-strand	122	1	8
α-helix	123-124	2
β-strand	125-129	5	4
α-helix	130-132	3
α-helix	133-139	7
β-strand	141-151	11	4
β-strand	152	1	8
β-strand	156-162	7	9
β-strand	165-167	3	9
β-strand	171-173	3	4
β-strand	178-179	2	4
β-strand	189-198	10	4
α-helix	199-203	5
β-strand	208-215	8	9
β-strand	218	1	10
α-helix	229-230	2
β-strand	232	1	10
β-strand	234-241	8	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
DMF5 alpha chain	A, D	protein	202	Homo sapiens	P01848 (AlphaFold model)
DMF5 beta chain	B, E	protein	243	Homo sapiens

Sequence of entity 1 (A, D), FASTA

>3QEU_1 DMF5 alpha chain (chains A, D)
AKEVEQNSGPLSVPEGAIASLNCTYSDRGSQSFFWYRQYSGKSPELIMFIYSNGDKEDGR
FTAQLNKASQYVSLLIRDSQPSDSATYLCAVNFGGGKLIFGQGTELSVKPNIQNPDPAVY
QLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVAWSNKSD
FACANAFNNSIIPEDTFFPSPE

Sequence of entity 2 (B, E), FASTA

>3QEU_2 DMF5 beta chain (chains B, E)
MIAGITQAPTSQILAAGRRMTLRCTQDMRHNAMYWYRQDLGLGLRLIHYSNTAGTTGKGE
VPDGYSVSRANTDDFPLTLASAVPSQTSVYFCASSLSFGTEAFFGQGTRLTVVEDLNKVF
PPEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVCTDPQPLKEQP
ALNDSRYALSSRLRVSATFWQDPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWG
RAD

Ligands and cofactors

ID	Name	Formula	Copies
LI	Lithium ion	Li	1

Water and common crystallization additives (GOL) are not listed.

Primary citation

TCRs Used in Cancer Gene Therapy Cross-React with MART-1/Melan-A Tumor Antigens via Distinct Mechanisms. Borbulevych, O.Y., Santhanagopolan, S.M., Hossain, M. et al. J Immunol (2011) 187:2453-2463. DOI 10.4049/jimmunol.1101268 · PubMed

Other PDB entries of the same protein (UniProt P01848 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4UDT 1.35 Å, T cell receptor (TRAV22,TRBV7-9) structure
4WW1 1.38 Å, Crystal structure of human TCR Alpha Chain-TRAV21-TRAJ8 and Beta Chain-TRBV7-8
1OGA 1.4 Å, A structural basis for immunodominant human T-cell receptor recognition.
2BNU 1.4 Å, Structural and kinetic basis for heightened immunogenicity of T cell vaccines
1KGC 1.5 Å, Immune Receptor
2BNQ 1.7 Å, Structural and kinetic basis for heightened immunogenicity of T cell vaccines
2BNR 1.9 Å, Structural and kinetic basis for heightened immunogenicity of T cell vaccines
2IAL 1.92 Å, Structural basis for recognition of mutant self by a tumor-specific, MHC class…
5C0C 1.97 Å, 1E6 TCR in complex with HLA-A02 carrying RQFGPDWIVA
2VLM 1.98 Å, The Structural Dynamics and Energetics of an Immunodominant T-cell Receptor are…
5KSA 2.0 Å, Bel602-DQ8.5-glia-gamma1 complex
7RYL 2.0 Å, T cell receptor CO3

Browse structure collections

About this viewer

MolViewer shows 3QEU 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.