9O07: Human MAIT A-F7 TCR

Structure of human MAIT A-F7 TCR in complex with human MR1-lumiflavin. Determined by X-ray diffraction at 1.97 Å resolution. Released 19 Nov 2025.

Method: X-ray diffraction
Resolution: 1.97 Å
Organism: Homo sapiens
Chains: 8
Atoms: 14,488
Mol. weight: 188.73 kDa
Ligands: LFN
Released: 19 Nov 2025

Explore 9O07 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9O07 contains 52 α-helices and 148 β-strands across 8 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: 10 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	3-12	10	19
α-helix	15-16	2
β-strand	22-28	7	19
β-strand	31-37	7	19
β-strand	44-45	2	19
α-helix	48-51	4
α-helix	56-84	29
β-strand	91-100	10	19
β-strand	106-114	9	19
β-strand	117-123	7	19
β-strand	128-131	4	19
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	20
α-helix	181-182	2
β-strand	183-188	6	21
β-strand	197-205	9	21
β-strand	206	1	20
β-strand	211-216	6	22
β-strand	219-220	2	22
β-strand	225-227	3	21
α-helix	228-230	3
β-strand	231-232	2	21
β-strand	238-245	8	21
β-strand	254-260	7	22
β-strand	263-268	6	22

Chain B: 6 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	3-5	3	23
β-strand	9-13	5	24
β-strand	18-25	8	23
β-strand	32-37	6	24
β-strand	44-49	6	24
β-strand	53-57	5	23
β-strand	60-65	6	23
β-strand	70-75	6	23
α-helix	80-82	3
β-strand	84-91	8	24
β-strand	97-99	3	24
β-strand	103-108	6	24
β-strand	117-120	4	25
α-helix	121-124	4
β-strand	130-135	6	25
α-helix	144-146	3
β-strand	152-153	2	25
α-helix	154-156	3
β-strand	157-161	5	25
α-helix	162-164	3
β-strand	166-175	10	25
α-helix	182-185	4
β-strand	196	1	25

Chain C: 8 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	48-51	4
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
α-helix	181-182	2
β-strand	183-190	8	3
β-strand	196-205	10	3
β-strand	206	1	2
β-strand	211-216	6	4
β-strand	220-221	2	4
β-strand	226-227	2	3
β-strand	231-232	2	3
β-strand	238-246	9	3
β-strand	254-260	7	4
β-strand	263-268	6	4

Chain D: 5 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	3-5	3	5
β-strand	9-13	5	6
β-strand	18-25	8	5
β-strand	32-37	6	6
β-strand	44-49	6	6
β-strand	53-57	5	5
β-strand	60-65	6	5
β-strand	70-75	6	5
α-helix	80-82	3
β-strand	84-91	8	6
α-helix	96	1
β-strand	97-99	3	6
β-strand	103-108	6	6
β-strand	117-121	5	7
β-strand	122	1	8
β-strand	131-135	5	7
α-helix	144-146	3
β-strand	152-153	2	7
α-helix	154-156	3
β-strand	157-161	5	7
α-helix	162-164	3
β-strand	166-174	9	7
β-strand	196	1	7

Chain E: 9 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	9
β-strand	10-14	5	10
β-strand	19-21	3	11
β-strand	22-25	4	9
β-strand	31-37	7	10
β-strand	44-51	8	10
β-strand	54-57	4	10
β-strand	64-68	5	11
β-strand	73	1	9
β-strand	74-78	5	11
α-helix	83-85	3
β-strand	87-94	8	10
α-helix	102-104	3
β-strand	105-106	2	10
β-strand	110-115	6	10
α-helix	118-120	3
β-strand	122	1	12
α-helix	123-124	2
β-strand	125-129	5	13
β-strand	130	1	8
α-helix	131-132	2
α-helix	133-139	7
β-strand	141-151	11	13
β-strand	152	1	12
β-strand	156-162	7	14
β-strand	165-167	3	14
β-strand	171-173	3	13
α-helix	177	1
β-strand	178-179	2	13
β-strand	189-198	10	13
α-helix	199-202	4
β-strand	208-215	8	14
β-strand	218	1	15
α-helix	229-230	2
β-strand	232	1	15
β-strand	234-241	8	14

Chain F: 2 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	16
α-helix	4-5	2
β-strand	6-11	6	17
β-strand	21-30	10	17
β-strand	31	1	16
β-strand	36-41	6	18
β-strand	44-45	2	18
β-strand	50-51	2	17
α-helix	52-54	3
β-strand	55-56	2	17
β-strand	62-70	9	17
β-strand	78-83	6	18
β-strand	91-94	4	18

Chain G: 9 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	26
β-strand	10-14	5	27
β-strand	19-21	3	28
β-strand	22-25	4	26
β-strand	31-37	7	27
β-strand	44-51	8	27
β-strand	54-57	4	27
β-strand	64-68	5	28
β-strand	73	1	26
β-strand	74-78	5	28
α-helix	83-85	3
β-strand	87-94	8	27
α-helix	102-104	3
β-strand	105-106	2	27
β-strand	110-115	6	27
α-helix	118-120	3
β-strand	122	1	29
α-helix	123-124	2
β-strand	125-129	5	30
α-helix	130-132	3
α-helix	133-139	7
β-strand	141-151	11	30
β-strand	152	1	29
β-strand	156-162	7	31
β-strand	165-167	3	31
β-strand	171-173	3	30
α-helix	177	1
β-strand	178-179	2	30
β-strand	189-198	10	30
α-helix	199-202	4
β-strand	208-215	8	31
β-strand	218	1	32
α-helix	229-230	2
β-strand	232	1	32
β-strand	234-241	8	31

Chain H: 3 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	33
α-helix	4-5	2
β-strand	6-11	6	34
β-strand	21-30	10	34
β-strand	31	1	33
β-strand	36-41	6	35
β-strand	44-45	2	35
α-helix	46	1
β-strand	50-51	2	34
α-helix	52-54	3
β-strand	55-56	2	34
β-strand	62-70	9	34
β-strand	78-83	6	35
β-strand	91-94	4	35

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Major histocompatibility complex class I-related gene protein	A, C	protein	271	Homo sapiens	Q95460 (AlphaFold model)
TCR-alpha	B, D	protein	204	Homo sapiens
TCR-beta	E, G	protein	246	Homo sapiens
Beta-2-microglobulin	F, H	protein	100	Homo sapiens	P61769 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>9O07_1 Major histocompatibility complex class I-related gene protein (chains A, C)
MRTHSLRYFRLGVSDPIHGVPEFISVGYVDSHPITTYDSVTRQKEPRAPWMAENLAPDHW
ERYTQLLRGWQQMFKVELKRLQRHYNHSGSHTYQRMIGCELLEDGSTTGFLQYAYDGQDF
LIFNKDTLSWLAVDNVAHTIKQAWEANQHELLYQKNWLEEECIAWLKRFLEYGKDTLQRT
EPPLVRVNRKETFPGVTALFCKAHGFYPPEIYMTWMKNGEEIVQEIDYGDILPSGDGTYQ
AWASIELDPQSSNLYSCHVEHSGVHMVLQVP

Sequence of entity 2 (B, D), FASTA

>9O07_2 TCR-alpha (chains B, D)
MGQNIDQPTEMTATEGAIVQINCTYQTSGFNGLFWYQQHAGEAPTFLSYNVLDGLEEKGR
FSSFLSRSKGYSYLLLKELQMKDSASYLCAVKDSNYQLIWGAGTKLIIKPDIQNPDPAVY
QLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVAWSNKSD
FACANAFNNSIIPEDTFFPSPESS

Sequence of entity 3 (E, G), FASTA

>9O07_3 TCR-beta (chains E, G)
MNAGVTQTPKFQVLKTGQSMTLQCAQDMNHNSMYWYRQDPGMGLRLIYYSASEGTTDKGE
VPNGYNVSRLNKREFSLRLESAAPSQTSVYFCASSVWTGEGSGELFFGEGSRLTVLEDLK
NVFPPEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVCTDPQPLK
EQPALNDSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAE
AWGRAD

Sequence of entity 4 (F, H), FASTA

>9O07_4 Beta-2-microglobulin (chains F, H)
MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD
WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM

Ligands and cofactors

ID	Name	Formula	Copies
LFN	Lumiflavin	C13 H12 N4 O2	2

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

Primary citation

The antigen-presenting molecule MR1 binds host-generated riboflavin catabolites. Abdelaal, M.R., Deng, J., McInerney, M.P. et al. J Exp Med (2026) 223. DOI 10.1084/jem.20250711 · 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
7ZT7 1.84 Å, Structure of E8 TCR in complex in human MR1 bound to 5FSA
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

Browse structure collections

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