7ZT7: E8 TCR in complex in human MR1

Structure of E8 TCR in complex in human MR1 bound to 5FSA. Determined by X-ray diffraction at 1.84 Å resolution. Released 28 Jun 2023.

Method: X-ray diffraction
Resolution: 1.84 Å
Organism: Homo sapiens
Chains: 4
Atoms: 6,826
Mol. weight: 98.19 kDa
Ligands: 54G
Released: 28 Jun 2023

Explore 7ZT7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7ZT7 contains 27 α-helices and 74 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: 9 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	3-12	10	1
β-strand	22-28	7	1
β-strand	31-37	7	1
β-strand	44-45	2	1
α-helix	48-53	6
α-helix	56-84	29
β-strand	91-100	10	1
β-strand	106-114	9	1
β-strand	117-123	7	1
β-strand	128-131	4	1
α-helix	134-144	11
α-helix	147-155	9
α-helix	156-160	5
α-helix	161-171	11
α-helix	173-176	4
β-strand	180	1	2
β-strand	183-192	10	3
β-strand	195-205	11	3
β-strand	206	1	2
β-strand	211-216	6	4
β-strand	221	1	4
α-helix	222	1
β-strand	226-227	2	3
β-strand	231-232	2	3
β-strand	238-245	8	3
α-helix	246-247	2
β-strand	254-260	7	4
β-strand	263-268	6	4

Chain B: 2 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	36-41	6	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	78-83	6	7
β-strand	91-94	4	7

Chain D: 7 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	5-7	3	8
β-strand	11-15	5	9
β-strand	20-27	8	8
β-strand	33-39	7	9
β-strand	46-51	6	9
β-strand	55-59	5	8
β-strand	62-67	6	8
β-strand	72-77	6	8
α-helix	82-84	3
β-strand	86-93	8	9
β-strand	99-101	3	9
β-strand	105-110	6	9
α-helix	111	1
β-strand	119-122	4	10
α-helix	123	1
β-strand	124	1	11
α-helix	125-126	2
β-strand	132-137	6	10
α-helix	146-148	3
β-strand	153-155	3	10
α-helix	156-158	3
β-strand	159-163	5	10
α-helix	164-166	3
β-strand	168-177	10	10

Chain E: 9 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	12
β-strand	10-14	5	13
β-strand	19-21	3	14
β-strand	22-25	4	12
β-strand	31-37	7	13
β-strand	44-51	8	13
β-strand	54-57	4	13
β-strand	64-66	3	14
β-strand	73	1	12
β-strand	76-78	3	14
α-helix	83-85	3
β-strand	87-94	8	13
α-helix	100-101	2
β-strand	102-103	2	13
β-strand	107-112	6	13
α-helix	115-117	3
β-strand	119	1	15
α-helix	120-121	2
β-strand	122-126	5	16
β-strand	127	1	11
α-helix	128-129	2
α-helix	130-136	7
β-strand	138-148	11	16
β-strand	149	1	15
β-strand	153-159	7	17
β-strand	162-164	3	17
β-strand	168-170	3	16
α-helix	174	1
β-strand	175-176	2	16
β-strand	186-195	10	16
α-helix	196-200	5
β-strand	205-212	8	17
β-strand	215	1	18
α-helix	226-227	2
β-strand	229	1	18
β-strand	231-238	8	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Major histocompatibility complex class I-related gene protein	A	protein	290	Homo sapiens	Q95460 (AlphaFold model)
Beta-2-microglobulin	B	protein	100	Homo sapiens	P61769 (AlphaFold model)
TCR alpha	D	protein	205	Homo sapiens
TCR beta	E	protein	262	Homo sapiens

Sequence of entity 1 (A), FASTA

>7ZT7_1 Major histocompatibility complex class I-related gene protein (chains A)
MRTHSLRYFRLGVSDPIHGVPEFISVGYVDSHPITTYDSVTRQKEPRAPWMAENLAPDHW
ERYTQLLRGWQQMFKVELKRLQRHYNHSGSHTYQRMIGCELLEDGSTTGFLQYAYDGQDF
LIFNKDTLSWLAVDNVAHTIKQAWEANQHELLYQKNWLEEECIAWLKRFLEYGKDTLQRT
EPPLVRVNRKETFPGVTALFCKAHGFYPPEIYMTWMKNGEEIVQEIDYGDILPSGDGTYQ
AWASIELDPQSSNLYSCHVEHSGVHMVLQVPGSGGGLNDIFEAQKIEWHE

Sequence of entity 2 (B), FASTA

>7ZT7_2 Beta-2-microglobulin (chains B)
MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD
WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM

Sequence of entity 3 (D), FASTA

>7ZT7_3 TCR alpha (chains D)
MAGQNIDQPTEMTATEGAIVQINCTYQTSGFNGLFWYQQHAGEAPTFLSYNVLDGLEEKG
RFSSFLSRSKGYSYLLLKELQMKDSASYLCAFLDSNYQLIWGAGTKLIIKPDIQNPDPAV
YQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVAWSNKS
DFACANAFNNSIIPEDTFFPSPESS

Sequence of entity 4 (E), FASTA

>7ZT7_4 TCR beta (chains E)
NAGVTQTPKFQVLKTGQSMTLQCAQDMNHNYMYWYRQDPGMGLRLIYYSASEGTTDKGEV
PNGYNVSRSTTEDFPLRLLSAAPSQTSVYFCASSNREYSPLHFGNGTRLTVTEDLNKVFP
PEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVCTDPQPLKEQPA
LNDSRYALSSRLRVSATFWQDPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGR
ADAAAGAAEQKLISEEDLNGAA

Ligands and cofactors

ID	Name	Formula	Copies
54G	2-hydroxy-5-methylbenzoic acid	C8 H8 O3	1

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

Primary citation

Promiscuous recognition of MR1 drives self-reactive mucosal-associated invariant T cell responses. Chancellor, A., Alan Simmons, R., Khanolkar, R.C. et al. J Exp Med (2023) 220. DOI 10.1084/jem.20221939 · PubMed

Other PDB entries of the same protein (UniProt Q95460 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6PUD 1.8 Å, Structure of human MAIT A-F7 TCR in complex with human MR1-5'OH-Pentyl-5-OP-U
6PUG 1.8 Å, Structure of human MAIT A-F7 TCR in complex with human MR1-2`OH-Ethyl-5-OP-U
6PUL 1.84 Å, Structure of human MAIT A-F7 TCR in complex with human MR1 3'D-5-OP-RU
6PUC 1.85 Å, Structure of human MAIT A-F7 TCR in complex with human MR1-5-OP-RU
6PUH 1.88 Å, Structure of human MAIT A-F7 TCR in complex with human MR1-Ribityl-less
6W9U 1.89 Å, Structure of human MAIT A-F7 TCR in complex with patient MR1-R9H-Ac-6-FP
4L4V 1.9 Å, Structure of human MAIT TCR in complex with human MR1-RL-6-Me-7-OH
5U6Q 1.9 Å, Structure of human MR1-3-F-SA in complex with human MAIT A-F7 TCR
6PUE 1.9 Å, Structure of human MAIT A-F7 TCR in complex with human MR1-4'D-5-OP-RU
6PUF 1.92 Å, Structure of human MAIT A-F7 TCR in complex with human MR1-5'D-5-OP-RU
6PUJ 1.92 Å, Structure of human MAIT A-F7 TCR in complex with human MR1-3`OH-Propyl-5-OP-U
4PJE 1.95 Å, Structure of human MR1-Ac-6-FP in complex with human MAIT B-B10 TCR

Browse structure collections

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