2F53: HLA class I histocompatibility antigen

Directed Evolution of Human T-cell Receptor CDR2 residues by phage display dramatically enhances affinity for cognate peptide-MHC without apparent cross-reactivity. Determined by X-ray diffraction at 2.1 Å resolution. Released 25 Apr 2006.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 5
Atoms: 7,335
Mol. weight: 93.67 kDa
Released: 25 Apr 2006

Explore 2F53 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2F53 contains 25 α-helices and 72 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: 12 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	139-149	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	2
α-helix	184-185	2
β-strand	186-192	7	3
β-strand	198-208	11	3
β-strand	209	1	2
β-strand	214-219	6	4
β-strand	222-223	2	4
α-helix	225-227	3
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

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: 4 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	3-4	2	8
β-strand	9-13	5	9
β-strand	18-24	7	8
β-strand	29-37	9	9
β-strand	43-50	8	9
β-strand	55-58	4	8
β-strand	61-66	6	8
α-helix	67-69	3
β-strand	71-76	6	8
α-helix	81-83	3
β-strand	85-93	9	9
β-strand	102-103	2	9
β-strand	107-112	6	9
β-strand	121-127	7	10
β-strand	134-139	6	10
β-strand	155-157	3	10
α-helix	158-160	3
β-strand	161-165	5	10
α-helix	166-168	3
β-strand	170-179	10	10

Chain E: 7 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	2-5	4	11
β-strand	8-12	5	12
β-strand	17-19	3	13
β-strand	20-23	4	11
β-strand	29-35	7	12
β-strand	41-49	9	12
β-strand	52-55	4	12
β-strand	62-64	3	13
β-strand	71	1	11
β-strand	74-76	3	13
α-helix	81-83	3
β-strand	85-92	8	12
β-strand	101-102	2	12
β-strand	106-111	6	12
α-helix	114-116	3
β-strand	118	1	14
α-helix	119-120	2
β-strand	121-126	6	10
α-helix	127-128	2
α-helix	129-135	7
β-strand	137-147	11	10
β-strand	148	1	14
β-strand	152-158	7	15
β-strand	161-163	3	15
β-strand	167-169	3	10
β-strand	174-175	2	10
β-strand	185-194	10	10
α-helix	195-198	4
β-strand	204-211	8	15
β-strand	214	1	16
α-helix	225-226	2
β-strand	228	1	16
β-strand	230-237	8	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
HLA class I histocompatibility antigen	A	protein	275	Homo sapiens	A0A140T913 (AlphaFold model)
Beta-2-microglobulin	B	protein	100	Homo sapiens	P61769 (AlphaFold model)
Cancer/testis antigen 1B	C	protein	9		P78358 (AlphaFold model)
T-cell Receptor, alpha chain	D	protein	193	Homo sapiens	A0A0B4J279 (AlphaFold model)
T-cell receptor, beta chain	E	protein	243	Homo sapiens	P01850

Sequence of entity 1 (A), FASTA

>2F53_1 HLA class I histocompatibility antigen (chains A)
GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYW
DGETRKVKAHSQTHRVDLGTLRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDG
KDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYLEGTCVEWLRRYLENGKETLQ
RTDAPKTHMTHHAVSDHEATLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT
FQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWE

Sequence of entity 2 (B), FASTA

>2F53_2 Beta-2-microglobulin (chains B)
MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD
WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPCIVKWDRDM

Sequence of entity 3 (C), FASTA

>2F53_3 Cancer/testis antigen 1B (chains C)
SLLMWITQC

Sequence of entity 4 (D), FASTA

>2F53_4 T-cell Receptor, alpha chain (chains D)
MKQEVTQIPAALSVPEGENLVLNCSFTDSAIYNLQWFRQDPGKGLTSLLLIPFWQREQTS
GRLNASLDKSSGRSTLYIAASQPGDSATYLCAVRPTSGGSYIPTFGRGTSLIVHPYIQNP
DPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVAW
SNKSDFACANAFN

Sequence of entity 5 (E), FASTA

>2F53_5 T-cell receptor, beta chain (chains E)
NAGVTQTPKFQVLKTGQSMTLQCAQDMNHEYMSWYRQDPGMGLRLIHYSVSVGMTDQGEV
PNGYNVSRSTTEDFPLRLLSAAPSQTSVYFCASSYVGNTGELFFGEGSRLTVLEDLKNVF
PPEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVCTDPQPLKEQP
ALNDSRYALSSRLRVSATFWQDPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWG
RAD

Primary citation

Directed evolution of human T cell receptor CDR2 residues by phage display dramatically enhances affinity for cognate peptide-MHC without increasing apparent cross-reactivity. Dunn, S.M., Rizkallah, P.J., Baston, E. et al. Protein Sci (2006) 15:710-721. DOI 10.1110/ps.051936406 · PubMed

Other PDB entries of the same protein (UniProt A0A140T913 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6O53 1.4 Å, Structure of HLA-A2:01 with peptide MM96
6O4Z 1.5 Å, Structure of HLA-A2:01 with peptide MM92
7QPJ 1.54 Å, Crystal structure of engineered TCR (756) complexed to HLA-A*02:01 presenting MAGE-A10…
6O51 1.55 Å, Structure of HLA-A2:01 with peptide MM90
6O4Y 1.58 Å, Structure of HLA-A2:01 with peptide MM91
7MJ7 1.6 Å, HLA-A*02:01 bound to Neuroblastoma Derived IGFBPL1 peptide
7P3D 1.67 Å, MHC I A02 Allele presenting YLQPRTFLL
7MJ9 1.75 Å, HLA-A*02:01 bound to Neuroblastoma Derived mutant IGFBPL1 peptide
7MJ8 1.79 Å, HLA-A*02:01 bound to Neuroblastoma Derived IGFBPL1 peptide
7SA2 1.85 Å, SARS-CoV-2 spike-derived peptide S1060-1068 (VVFLHVTYV) presented by HLA-A*02:01
2P5E 1.89 Å, Crystal Structures of High Affinity Human T-Cell Receptors Bound to pMHC Reveal Native…
7MKB 1.9 Å, Human leukocyte antigen A*0201 in complex with SARS-CoV-2 epitope YLQPRTFLL

Browse structure collections

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