3ERY: H-2 class I histocompatibility antigen

Different thermodynamic binding mechanisms and peptide fine specificities associated with a panel of structurally similar high-affinity T cell receptors. Determined by X-ray diffraction at 1.95 Å resolution. Released 25 Nov 2008.

Method: X-ray diffraction
Resolution: 1.95 Å
Organism: Homo sapiens
Chains: 4
Atoms: 2,946
Mol. weight: 43.1 kDa
Released: 25 Nov 2008

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

Secondary structure: helices and β-sheets

3ERY contains 13 α-helices and 15 β-strands across 3 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: 6 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	3-12	10	1
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	165-173	9

Chain B: 6 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	3-12	10	2
α-helix	13-14	2
α-helix	19-20	2
β-strand	21-28	8	2
β-strand	31-37	7	2
α-helix	65-84	20
β-strand	94-103	10	2
β-strand	109-118	10	2
β-strand	121-126	6	2
β-strand	133-135	3	2
α-helix	138-150	13
α-helix	152-158	7
α-helix	162-169	8

Chain P: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	2-8	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
H-2 class I histocompatibility antigen	A, B	protein	174	Homo sapiens	P01897 (AlphaFold model)
2-oxoglutarate dehydrogenase E1 peptide	P, Q	protein	9		Q02218 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3ERY_1 H-2 class I histocompatibility antigen (chains A, B)
GPHSMRYYETATSRRGLGEPRYTSVGYVDDKEFVRFDSDAENPRYEPQVPWMEQEGPEYW
ERITQVAKGQEQWFRVNLRTLLGYYNQSAGGTHTLQRMYGCDVGSDGRLLRGYEQFAYDG
CDYIALNEDLRTWTAADMAAQITRRKWEQAGAAEYYRAYLEGECVEWLHRYLKN

Sequence of entity 2 (P, Q), FASTA

>3ERY_2 2-oxoglutarate dehydrogenase E1 peptide (chains P, Q)
QLSPFPFDL

Primary citation

Different thermodynamic binding mechanisms and peptide fine specificities associated with a panel of structurally similar high-affinity T cell receptors. Jones, L.L., Colf, L.A., Bankovich, A.J. et al. Biochemistry (2008) 47:12398-12408. DOI 10.1021/bi801349g · PubMed

Other PDB entries of the same protein (UniProt P01897 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3V4U 1.64 Å, Structure of a monoclonal antibody complexed with its MHC-I antigen
3UO1 1.64 Å, Structure of a monoclonal antibody complexed with its MHC-I antigen
3V52 1.7 Å, Structure of a monoclonal antibody complexed with its MHC-I antigen
3UYR 1.7 Å, Structure of a monoclonal antibody complexed with its MHC-I antigen
6L9K 1.8 Å, H2-Ld a1a2 complexed with A5 peptide
8D5N 1.8 Å, Crystal structure of Ld-HF10
3VJ6 1.9 Å, Structure of the MHC class Ib molecule Qa-1b
4MS8 1.92 Å, 42F3 TCR pCPB9/H-2Ld Complex
5VCL 2.05 Å, Structure of the Qdm peptide bound to Qa-1a
3TJH 2.12 Å, 42F3-p3A1/H2-Ld complex
2OI9 2.35 Å, Structure of the 2C/Ld/QL9 allogeneic complex
6L9L 2.4 Å, 1D4 TCR recognition of H2-Ld a1a2 A5 Peptide Complexes

Browse structure collections

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