8RYQ: S8-9F3 TCR

Structure of S8-9F3 TCR in complex with HLA-A*11:01 bound to ELFSYLIEK peptide. Determined by X-ray diffraction at 2.49 Å resolution. Released 4 Sept 2024.

Method: X-ray diffraction
Resolution: 2.49 Å
Organism: Homo sapiens
Chains: 10
Atoms: 13,006
Mol. weight: 188.65 kDa
Released: 4 Sept 2024

Explore 8RYQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8RYQ contains 45 α-helices and 142 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.

Chains A and F: 10 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	3-12	10	1
α-helix	20	1
β-strand	21-28	8	1
β-strand	31-37	7	1
β-strand	46-47	2	1
α-helix	50-54	5
α-helix	57-84	28
β-strand	94-103	10	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	152-161	10
α-helix	163-174	12
α-helix	176-179	4
β-strand	183	1	2
α-helix	184-185	2
β-strand	186-193	8	3
β-strand	198-208	11	3
β-strand	209	1	2
β-strand	214-219	6	4
β-strand	222-224	3	4
β-strand	228-230	3	3
α-helix	231-233	3
β-strand	234-235	2	3
β-strand	241-250	10	3
α-helix	254-256	3
β-strand	257-262	6	4
β-strand	270-272	3	4

Chains B and G: 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
α-helix	46	1
β-strand	50-51	2	6
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: 3 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	5-6	2	8
β-strand	11-15	5	9
β-strand	20-26	7	8
β-strand	31-39	9	9
β-strand	45-52	8	9
β-strand	57-60	4	8
β-strand	63-68	6	8
β-strand	73-78	6	8
α-helix	83-85	3
β-strand	87-95	9	9
β-strand	103-104	2	9
β-strand	108-113	6	9
β-strand	122-127	6	10
β-strand	128	1	11
β-strand	135-140	6	10
α-helix	149-151	3
β-strand	156-158	3	10
α-helix	159-161	3
β-strand	162-166	5	10
β-strand	171-180	10	10

Chains E and J: 8 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	6-8	3	12
β-strand	11-15	5	13
β-strand	20-25	6	12
α-helix	26-27	2
β-strand	32-39	8	13
β-strand	43-51	9	13
β-strand	54-58	5	13
β-strand	65-69	5	12
β-strand	75-79	5	12
α-helix	84-86	3
β-strand	88-95	8	13
β-strand	104-105	2	13
α-helix	106	1
β-strand	109-114	6	13
β-strand	121	1	14
α-helix	122-123	2
β-strand	124-128	5	11
α-helix	129-131	3
α-helix	132-138	7
β-strand	140-150	11	11
β-strand	151	1	14
β-strand	155-161	7	15
β-strand	164-166	3	15
β-strand	170-172	3	11
β-strand	177-178	2	11
α-helix	186-187	2
β-strand	188-197	10	11
α-helix	198-202	5
β-strand	207-214	8	15
β-strand	217	1	16
β-strand	231	1	16
β-strand	233-240	8	15

Chain I: 2 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	5-6	2	24
β-strand	11-15	5	25
β-strand	20-26	7	24
β-strand	31-39	9	25
β-strand	45-52	8	25
β-strand	57-60	4	24
β-strand	63-68	6	24
β-strand	73-78	6	24
α-helix	83-85	3
β-strand	87-95	9	25
β-strand	103-104	2	25
β-strand	108-113	6	25
β-strand	122-127	6	26
β-strand	128	1	27
β-strand	135-140	6	26
β-strand	156-158	3	26
α-helix	159-161	3
β-strand	162-166	5	26
β-strand	171-180	10	26

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
MHC class I antigen	A, F	protein	276	Homo sapiens	A0A583ZB34 (AlphaFold model)
Beta-2-microglobulin	B, G	protein	100	Homo sapiens	P61769 (AlphaFold model)
ELFSYLIEK peptide	C, H	protein	9	Homo sapiens
TCR alpha	D, I	protein	200	Homo sapiens
TCR beta	E, J	protein	244	Homo sapiens

Sequence of entity 1 (A, F), FASTA

>8RYQ_1 MHC class I antigen (chains A, F)
GSHSMRYFYTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYW
DQETRNVKAQSQTDRVDLGTLRGYYNQSEDGSHTIQIMYGCDVGPDGRFLRGYRQDAYDG
KDYIALNEDLRSWTAADMAAQITKRKWEAAHAAEQQRAYLEGRCVEWLRRYLENGKETLQ
RTDPPKTHMTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT
FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP

Sequence of entity 2 (B, G), FASTA

>8RYQ_2 Beta-2-microglobulin (chains B, G)
MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD
WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM

Sequence of entity 3 (C, H), FASTA

>8RYQ_3 ELFSYLIEK peptide (chains C, H)
ELFSYLIEK

Sequence of entity 4 (D, I), FASTA

>8RYQ_4 TCR alpha (chains D, I)
MKQEVTQIPAALSVPEGENLVLNCSFTDSAIYNLQWFRQDPGKGLTSLLLIQSSQREQTS
GRLNASLDKSSGRSTLYIAASQPGDSATYLCAVRQWGSLGNLIFGKGTKLSVKPNIQNPD
PAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVAWS
NKSDFACANAFNNSIIPEDT

Sequence of entity 5 (E, J), FASTA

>8RYQ_5 TCR beta (chains E, J)
MDSGVTQTPKHLITATGQRVTLRCSPRSGDLSVYWYQQSLDQGLQFLIQYYNGEERAKGN
ILERFSAQQFPDLHSELNLSSLELGDSALYFCASSPGGGHNEQFFGPGTRLTVLEDLKNV
FPPEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVCTDPQPLKEQ
PALNDSRYALSSRLRVSATFWQDPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAW
GRAD

Primary citation

Broadening alloselectivity of T cell receptors by structure guided engineering. Karuppiah, V., Sangani, D., Whaley, L. et al. Sci Rep (2024) 14:26851-26851. DOI 10.1038/s41598-024-75140-7 · PubMed

Other PDB entries of the same protein (UniProt A0A583ZB34 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7OW4 1.81 Å, Crystal structure of HLA-A*11:01 in complex with KRAS G12D peptide (VVVGADGVGK)
8RYN 1.97 Å, Structure of S2 TCR in complex with HLA-A*11:01 bound to ELFSYLIEK peptide
8WTE 2.17 Å, Crystal structure of TCR in complex with HLA-A*11:01 bound to KRAS-G12V peptide…
8WUL 2.36 Å, Crystal structure of affinity enhanced TCR in complex with HLA-A*11:01 bound to…
7OW3 2.46 Å, Crystal structure of HLA-A*11:01 in complex with KRAS peptide (VVVGAGGVGK)
7OW5 2.58 Å, Crystal structure of a TCR in complex with HLA-A*11:01 bound to KRAS peptide (VVVGAGGVGK)
7OW6 2.64 Å, Crystal structure of a TCR in complex with HLA-A*11:01 bound to KRAS G12D peptide…
7PB2 3.41 Å, Crystal structure of JDI TCR in complex with HLA-A*11:01 bound to KRAS G12D peptide…

Browse structure collections

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