3KXF: SB27 TCR

Crystal Structure of SB27 TCR in complex with the 'restriction triad' mutant HLA-B*3508-13mer. Determined by X-ray diffraction at 3.1 Å resolution. Released 9 Jun 2010.

Method: X-ray diffraction
Resolution: 3.1 Å
Organism: Homo sapiens
Chains: 20
Atoms: 26,991
Mol. weight: 384.87 kDa
Released: 9 Jun 2010

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

Secondary structure: helices and β-sheets

3KXF contains 90 α-helices and 305 β-strands across 20 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: 11 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	1
α-helix	19-20	2
β-strand	21-28	8	1
β-strand	31-37	7	1
β-strand	45-47	3	1
α-helix	50-52	3
α-helix	57-85	29
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	138-150	13
α-helix	152-157	6
α-helix	158-163	6
α-helix	164-174	11
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	214-218	5	4
β-strand	223	1	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	258-262	5	4
β-strand	271-272	2	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
α-helix	14-15	2
β-strand	21-30	10	6
β-strand	31	1	5
β-strand	35-41	7	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	78-84	7	7
β-strand	91-94	4	7

Chain C: 9 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	8
β-strand	21-28	8	8
β-strand	31-37	7	8
β-strand	46-47	2	8
α-helix	57-81	25
β-strand	94-103	10	8
β-strand	109-118	10	8
β-strand	121-126	6	8
β-strand	133-134	2	8
α-helix	138-148	11
α-helix	152-158	7
α-helix	159-163	5
α-helix	164-174	11
α-helix	176-179	4
β-strand	183	1	9
α-helix	184-185	2
β-strand	186-193	8	10
β-strand	198-208	11	10
β-strand	209	1	9
β-strand	214-219	6	11
β-strand	222-223	2	11
β-strand	229-230	2	10
α-helix	231-233	3
β-strand	234-235	2	10
β-strand	241-250	10	10
α-helix	254-256	3
β-strand	257-262	6	11
β-strand	270-272	3	11

Chain D: 3 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	2-4	3	12
β-strand	9-13	5	13
β-strand	18-20	3	12
β-strand	23-25	3	12
β-strand	32-38	7	13
β-strand	45-51	7	13
β-strand	57-60	4	12
β-strand	63-68	6	12
β-strand	73-78	6	12
α-helix	83-85	3
β-strand	87-94	8	13
β-strand	97	1	14
β-strand	103-104	2	13
β-strand	108-113	6	13
β-strand	122-126	5	15
β-strand	136-140	5	15
α-helix	149-151	3
β-strand	157-158	2	15
α-helix	159-161	3
β-strand	162-166	5	15
β-strand	171-179	9	15
β-strand	201	1	15

Chain E: 9 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	16
β-strand	10-14	5	17
β-strand	19-25	7	16
β-strand	32-37	6	17
β-strand	43-49	7	17
β-strand	56-57	2	17
β-strand	65-66	2	16
β-strand	73-78	6	16
α-helix	83-85	3
β-strand	87-92	6	17
α-helix	98-100	3
β-strand	104	1	17
β-strand	108-113	6	17
α-helix	116-118	3
β-strand	120	1	18
α-helix	121-122	2
β-strand	123-127	5	19
α-helix	128-130	3
α-helix	131-137	7
β-strand	139-149	11	19
β-strand	150	1	18
β-strand	154-160	7	20
β-strand	163-165	3	20
β-strand	169-171	3	19
α-helix	175	1
β-strand	176-177	2	19
β-strand	187-196	10	19
α-helix	197-200	4
β-strand	206-213	8	20
β-strand	216	1	21
α-helix	227-228	2
β-strand	230	1	21
β-strand	232-239	8	20

Chain F: 1 helix, 11 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	22
β-strand	6-11	6	23
β-strand	21-30	10	23
β-strand	31	1	22
β-strand	36-41	6	24
β-strand	44-45	2	24
β-strand	50-51	2	23
α-helix	52-54	3
β-strand	55-56	2	23
β-strand	62-70	9	23
β-strand	78-83	6	24
β-strand	91-94	4	24

Chain G: 3 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	2-4	3	25
β-strand	9-13	5	26
β-strand	18-20	3	25
β-strand	23-25	3	25
β-strand	32-38	7	26
β-strand	45-51	7	26
β-strand	58	1	25
β-strand	63-68	6	25
β-strand	73-78	6	25
α-helix	83-85	3
β-strand	87-94	8	26
β-strand	97	1	27
β-strand	102-104	3	26
β-strand	108-113	6	26
β-strand	122-126	5	28
β-strand	136-140	5	28
β-strand	156-158	3	28
β-strand	162-166	5	28
α-helix	167-169	3
β-strand	171-180	10	28
α-helix	187-190	4
β-strand	201	1	28

Chain H: 8 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	29
β-strand	10-14	5	30
β-strand	19-21	3	31
β-strand	22-25	4	29
β-strand	32-38	7	30
β-strand	42-49	8	30
β-strand	56-57	2	30
β-strand	65-67	3	31
β-strand	73	1	29
β-strand	75-78	4	31
α-helix	83-85	3
β-strand	87-92	6	30
α-helix	98-100	3
β-strand	104	1	30
β-strand	108-113	6	30
α-helix	116-118	3
β-strand	120	1	32
α-helix	121-122	2
β-strand	123-127	5	33
α-helix	128-130	3
α-helix	131-137	7
β-strand	139-149	11	33
β-strand	150	1	32
β-strand	154-160	7	34
β-strand	163-165	3	34
β-strand	169-171	3	33
β-strand	176-177	2	33
β-strand	187-196	10	33
α-helix	197-201	5
β-strand	206-213	8	34
β-strand	216	1	35
α-helix	227-228	2
β-strand	230	1	35
β-strand	232-239	8	34

10 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
HLA class I histocompatibility antigen, B-35 alpha chain	A, C, I, K	protein	276	Homo sapiens	P01889 (AlphaFold model)
Beta-2-microglobulin	B, F, J, L	protein	99	Homo sapiens	P61769 (AlphaFold model)
SB27 T cell receptor alpha chain	D, G, M, N	protein	204	Homo sapiens	P01848 (AlphaFold model)
SB27 T cell receptor beta chain	E, H, O, P	protein	241	Homo sapiens	A0A5B9 (AlphaFold model)
peptide from Trans-activator protein BZLF1	Q, R, S, T	protein	13		P03206

Sequence of entity 1 (A, C, I, K), FASTA

>3KXF_1 HLA class I histocompatibility antigen, B-35 alpha chain (chains A, C, I, K)
GSHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRTEPRAPWIEQEGPEYW
DRNTAIFKANTQTYRESLRNLRGYYNQSEAGSHIIQRMYGCDLGPDGRLLRGHDQSAYDG
KDYIALNEDLSSWTAADTAAQITQRKWEAARVAEARRAYLEGLCVEWLRRYLENGKETLQ
RADPPKTHVTHHPVSDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRT
FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP

Sequence of entity 2 (B, F, J, L), FASTA

>3KXF_2 Beta-2-microglobulin (chains B, F, J, L)
IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDW
SFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM

Sequence of entity 3 (D, G, M, N), FASTA

>3KXF_3 SB27 T cell receptor alpha chain (chains D, G, M, N)
QKVTQAQTEISVVEDEDVTLDCVYETRDTTYYLFWYKQPPSGELVFLIRRNSFDEQNEIS
GRYSWNFQKSTSSFNFTITASQVVDSAVYFCALSGFYNTDKLIFGTGTRLQVFPNIQNPD
PAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVAWS
NKSDFACANAFNNSIIPEDTFFPS

Sequence of entity 4 (E, H, O, P), FASTA

>3KXF_4 SB27 T cell receptor beta chain (chains E, H, O, P)
GVTQTPKFQVLKTGQSMTLQCAQDMNHNSMYWYRQDPGMGLRLIYYSASEGTTDKGEVPN
GYNVSRLNKREFSLRLESAAPSQTSVYFCASPGLAGEYEQYFGPGTRLTVTEDLKNVFPP
EVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVCTDPEPLKEQPAL
NDSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRA
D

Sequence of entity 5 (Q, R, S, T), FASTA

>3KXF_5 peptide from Trans-activator protein BZLF1 (chains Q, R, S, T)
LPEPLPQGQLTAY

Primary citation

Hard wiring of T cell receptor specificity for the major histocompatibility complex is underpinned by TCR adaptability. Burrows, S.R., Chen, Z., Archbold, J.K. et al. Proc Natl Acad Sci U S A (2010) 107:10608-10613. DOI 10.1073/pnas.1004926107 · 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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