2NW2: ELS4 TCR

Crystal structure of ELS4 TCR at 1.4A. Determined by X-ray diffraction at 1.4 Å resolution. Released 27 Feb 2007.

Method: X-ray diffraction
Resolution: 1.4 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,059
Mol. weight: 49.69 kDa
Released: 27 Feb 2007

Explore 2NW2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2NW2 contains 14 α-helices and 41 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: 7 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	4	1	1
β-strand	9-13	5	2
β-strand	18-23	6	1
β-strand	32-37	6	2
β-strand	44-49	6	2
β-strand	53-57	5	1
β-strand	62-67	6	1
β-strand	72-77	6	1
α-helix	82-84	3
β-strand	86-92	7	2
α-helix	104	1
β-strand	105-106	2	2
α-helix	107	1
β-strand	110-115	6	2
α-helix	116-117	2
β-strand	124-130	7	3
β-strand	137-142	6	3
β-strand	158-160	3	3
α-helix	161-163	3
β-strand	164-168	5	3
α-helix	169-171	3
β-strand	173-182	10	3
α-helix	189-192	4
β-strand	203	1	3

Chain B: 7 helices, 24 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	43-51	9	5
β-strand	54-57	4	5
β-strand	66-71	6	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
α-helix	120-122	3
β-strand	124	1	6
α-helix	125-126	2
β-strand	127-132	6	3
α-helix	133-134	2
α-helix	135-141	7
β-strand	143-153	11	3
β-strand	154	1	6
β-strand	158-164	7	7
β-strand	167-169	3	7
β-strand	173-175	3	3
β-strand	180-181	2	3
β-strand	191-200	10	3
α-helix	201-204	4
β-strand	210-217	8	7
β-strand	220	1	8
α-helix	231-232	2
β-strand	234	1	8
β-strand	236-243	8	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ELS4 TCR alpha chain	A	protein	200	Homo sapiens	Q6P4G7 (AlphaFold model)
ELS4 TCR beta chain	B	protein	243	Homo sapiens	P01850 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2NW2_1 ELS4 TCR alpha chain (chains A)
QNIDQPTEMTATEGAIVQINCTYQTSGFNGLFWYQQHAGEAPTFLSYNVLDGLEEKGRFS
SFLSRSKGYSYLLLKELQMKDSASYLCAVQASGGSYIPTFGRGTSLIVHPYIQNPDPAVY
QLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVAWSNKSD
FACANAFNNSIIPEDTFFPS

Sequence of entity 2 (B), FASTA

>2NW2_2 ELS4 TCR beta chain (chains B)
DAGITQSPRHKVTETGTPVTLRCHQTENHRYMYWYRQDPGHGLRLIHYSYGVKDTDKGEV
SDGYSVSRSKTEDFLLTLESATSSQTSVYFCATGTGDSNQPQHFGDGTRLSILEDLNKVF
PPEVAVFEPSEAEISHTQKATLVCLATGFFPDHVELSWWVNGKEVHSGVCTDPQPLKEQP
ALNDSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWG
RAD

Primary citation

A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule. Tynan, F.E., Reid, H.H., Kjer-Nielsen, L. et al. Nat Immunol (2007) 8:268-276. DOI 10.1038/ni1432 · PubMed

Other PDB entries of the same protein (UniProt Q6P4G7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4L4V 1.9 Å, Structure of human MAIT TCR in complex with human MR1-RL-6-Me-7-OH
4NQE 2.1 Å, Crystal structure of TCR-MR1 ternary complex bound to 5-(2-oxoethylideneamino)-6-D-ribity…
4NQD 2.2 Å, Crystal structure of TCR-MR1 ternary complex and non-covalently bound…
4LCW 2.4 Å, The structure of human MAIT TCR in complex with MR1-K43A-RL-6-Me-7OH
4NQC 2.5 Å, Crystal structure of TCR-MR1 ternary complex and covalently bound…
9C42 2.69 Å, Structure of human MR1-ellagic acid in complex with human MAIT A-F7 TCR
5WKI 2.75 Å, Crystal structure of PG90 TCR-CD1b-PG complex
4IIQ 2.86 Å, Crystal structure of a human MAIT TCR in complex with bovine MR1
4L8S 2.9 Å, Crystal structure of a human Valpha7.2/Vbeta13.3 MAIT TCR in complex with bovine MR1
4LCC 3.26 Å, Crystal structure of a human MAIT TCR in complex with a bacterial antigen bound to…
4L9L 3.4 Å, Crystal structure of a human Valpha7.2/Vbeta13.2 MAIT TCR in complex with bovine MR1

Browse structure collections

About this viewer

MolViewer shows 2NW2 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.