3MV7: TK3 TCR

Crystal Structure of the TK3 TCR in complex with HLA-B*3501/HPVG. Determined by X-ray diffraction at 2.0 Å resolution. Released 9 Jun 2010.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 5
Atoms: 7,407
Mol. weight: 94.48 kDa
Released: 9 Jun 2010

Explore 3MV7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3MV7 contains 30 α-helices and 71 β-strands across 5 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	1
α-helix	19-20	2
β-strand	21-28	8	1
β-strand	31-37	7	1
β-strand	46-47	2	1
α-helix	50-52	3
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	152-159	8
α-helix	160-164	5
α-helix	165-174	10
α-helix	176-179	4
β-strand	183	1	2
α-helix	184-185	2
β-strand	186-193	8	3
β-strand	199-208	10	3
β-strand	209	1	2
β-strand	214-219	6	4
β-strand	222-223	2	4
β-strand	228-230	3	3
α-helix	231-233	3
β-strand	234-235	2	3
β-strand	241-249	9	3
β-strand	257-262	6	4
β-strand	270-272	3	4

Chain B: 3 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
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 C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	2-5	4

Chain D: 7 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	8
β-strand	10-14	5	9
β-strand	19-25	7	8
β-strand	30-44	9	9
β-strand	51-56	6	9
β-strand	66-69	4	8
β-strand	79-83	5	8
β-strand	86-91	6	8
α-helix	92	1
α-helix	96-98	3
β-strand	100-108	9	9
β-strand	117-118	2	9
β-strand	122-127	6	9
α-helix	128-129	2
β-strand	136-142	7	10
β-strand	149-154	6	10
α-helix	162-165	4
β-strand	170-172	3	10
α-helix	173-175	3
β-strand	176-180	5	10
α-helix	181-183	3
β-strand	185-194	10	10
α-helix	201-203	3
β-strand	215	1	10

Chain E: 9 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	5-7	3	11
β-strand	10-14	5	12
β-strand	19-24	6	11
α-helix	25-26	2
β-strand	31-45	8	12
β-strand	50-57	8	12
β-strand	60-68	5	12
β-strand	76-80	5	11
β-strand	87-91	5	11
α-helix	96-98	3
β-strand	100-107	8	12
β-strand	113-115	3	12
β-strand	119-124	6	12
β-strand	131	1	13
α-helix	132-133	2
β-strand	134-139	6	10
α-helix	140-141	2
α-helix	142-148	7
β-strand	150-160	11	10
β-strand	161	1	13
β-strand	165-171	7	14
β-strand	174-176	3	14
β-strand	180-182	3	10
α-helix	186	1
β-strand	187-188	2	10
β-strand	198-207	10	10
α-helix	208-211	4
β-strand	217-224	8	14
α-helix	225	1
β-strand	227	1	15
α-helix	238-239	2
β-strand	241	1	15
β-strand	243-250	8	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
HLA class I histocompatibility antigen, B-35 alpha chain	A	protein	276	Homo sapiens	P01889 (AlphaFold model)
Beta-2-microglobulin	B	protein	99	Homo sapiens	P61769 (AlphaFold model)
HPVG peptide from Epstein-Barr nuclear antigen 1	C	protein	11		P03211 (AlphaFold model)
alpha chain of the TK3 TCR	D	protein	200	Homo sapiens
beta chain of the TK3 TCR	E	protein	241	Homo sapiens

Sequence of entity 1 (A), FASTA

>3MV7_1 HLA class I histocompatibility antigen, B-35 alpha chain (chains A)
GSHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRTEPRAPWIEQEGPEYW
DRNTQIFKTNTQTYRESLRNLRGYYNQSEAGSHIIQRMYGCDLGPDGRLLRGHDQSAYDG
KDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQLRAYLEGLCVEWLRRYLENGKETLQ
RADPPKTHVTHHPVSDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRT
FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP

Sequence of entity 2 (B), FASTA

>3MV7_2 Beta-2-microglobulin (chains B)
IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDW
SFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM

Sequence of entity 3 (C), FASTA

>3MV7_3 HPVG peptide from Epstein-Barr nuclear antigen 1 (chains C)
HPVGEADYFEY

Sequence of entity 4 (D), FASTA

>3MV7_4 alpha chain of the TK3 TCR (chains D)
QVTQSPEALRLQEGESSSLNCSYTVSGLRGLFWYRQDPGKGPEFLFTLYSAGEEKEKERL
KATLTKKESFLHITAPKPEDSATYLCAVQDLGTSGSRLTFGEGTQLTVNPNIQNPDPAVY
QLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVAWSNKSD
FACANAFNNSIIPEDTFFPS

Sequence of entity 5 (E), FASTA

>3MV7_5 beta chain of the TK3 TCR (chains E)
DSGVTQTPKHLITATGQRVTLRCSPRSGDLSVYWYQQSLDQGLQFLIQYYNGEERAKGNI
LERFSAQQFPDLHSELNLSSLELGDSALYFCASSARSGELFFGEGSRLTVLEDLKNVFPP
EVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVCTDPQPLKEQPAL
NDSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRA
D

Primary citation

Allelic polymorphism in the T cell receptor and its impact on immune responses. Gras, S., Chen, Z., Miles, J.J. et al. J Exp Med (2010) 207:1555-1567. DOI 10.1084/jem.20100603 · PubMed

Other PDB entries of the same protein (UniProt P01889 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1K5N 1.09 Å, HLA-B*2709 bound to nona-peptide M9
4U1M 1.18 Å, HLA class I micropolymorphisms determine peptide-HLA landscape and dictate differential…
3CZF 1.2 Å, Crystal structure of HLA-B*2709 complexed with the glucagon receptor (GR) peptide…
6MT3 1.21 Å, Crystal Structure of HLA-B*18:01 in complex with NP338 influenza peptide
3LN4 1.3 Å, Crystal structure of HLA-B*4103 in complex with a 16mer self-peptide derived from…
3BWA 1.3 Å, Crystal Structure of HLA B*3508 in complex with a HCMV 8-mer peptide from the pp65 protein
3SPV 1.3 Å, Crystal structure of a peptide-HLA complex
6MT6 1.31 Å, Crystal Structure of HLA-B*37:01 in complex with NP338 influenza peptide
2BVP 1.35 Å, Structures of Three HIV-1 HLA-B5703-Peptide Complexes and Identification of Related HLAs…
6MTL 1.35 Å, Crystal Structure of HLA-B*44:05 in complex with NP338 influenza peptide
4U1J 1.38 Å, HLA class I micropolymorphisms determine peptide-HLA landscape and dictate differential…
6PYW 1.38 Å, Crystal Structure of HLA-B*2705-W60A in complex with LRN, a self-peptide

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