1ES0: Murine class II allele I-A(G7)

Crystal structure of the murine class II allele I-A(G7) complexed with the glutamic acid decarboxylase (GAD65) peptide 207-220. Determined by X-ray diffraction at 2.6 Å resolution. Released 28 Jun 2000.

Method: X-ray diffraction
Resolution: 2.6 Å
Organisms: Mus musculus, Homo sapiens
Chains: 2
Atoms: 3,088
Mol. weight: 47.19 kDa
Released: 28 Jun 2000

Explore 1ES0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1ES0 contains 12 α-helices and 30 β-strands across 2 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: 4 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	4-15	12	1
β-strand	19-26	8	1
β-strand	29-35	7	1
β-strand	40-43	4	1
α-helix	48-50	3
β-strand	53	1	2
α-helix	56-76	21
α-helix	80-85	6
β-strand	88-93	6	3
β-strand	103-112	10	3
β-strand	118-123	6	4
β-strand	126-128	3	4
β-strand	132-134	3	3
α-helix	137	1
β-strand	138-139	2	3
β-strand	145-153	9	3
β-strand	160-166	7	4
β-strand	174-179	6	4

Chain B: 8 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	208P	1	2
α-helix	209P-219P	11
β-strand	7-18	12	1
β-strand	23-32	10	1
β-strand	35-41	7	1
β-strand	47-49	3	1
α-helix	55-74	18
α-helix	75-80	6
α-helix	81-82	2
α-helix	83-87	5
α-helix	91-93	3
β-strand	95	1	5
β-strand	98-103	6	6
β-strand	114-122	9	6
β-strand	123	1	5
β-strand	128-133	6	7
β-strand	136-137	2	7
α-helix	138	1
β-strand	142-144	3	6
α-helix	145-147	3
β-strand	148-149	2	6
β-strand	155-162	8	6
β-strand	171-176	6	7
β-strand	184-188	5	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
H-2 class II histocompatibility antigen	A	protein	190	Mus musculus	P04228 (AlphaFold model)
65 kd glutamic acid decarboxylase+h-2 class II histocompatibility antigen	B	protein	221	Homo sapiens	Q05329 (AlphaFold model), Q31135 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1ES0_1 H-2 CLASS II HISTOCOMPATIBILITY ANTIGEN (chains A)
EDDIEADHVGFYGTTVYQSPGDIGQYTHEFDGDELFYVDLDKKKTVWRLPEFGQLILFEP
QGGLQNIAAEKHNLGILTKRSNFTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPV
INITWLRNSKSVTDGVYETSFLVNRDHSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLK
HWSSADLVPR

Sequence of entity 2 (B), FASTA

>1ES0_2 65 KD GLUTAMIC ACID DECARBOXYLASE+H-2 CLASS II HISTOCOMPATIBILITY ANTIGEN (chains B)
GSHSRGYEIAPVFVLLEYVTGSGSGSGDSERHFVHQFKGECYFTNGTQRIRLVTRYIYNR
EEYLRFDSDVGEYRAVTELGRHSAEYYNKQYLERTRAELDTACRHNYEETEVPTSLRRLE
QPNVAISLSRTEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLIRNGDWTF
QVLVMLEMTPHQGEVYTCHVEHPSLKSPITVEWSSADLVPR

Primary citation

A structural framework for deciphering the link between I-Ag7 and autoimmune diabetes. Corper, A.L., Stratmann, T., Apostolopoulos, V. et al. Science (2000) 288:505-511. DOI 10.1126/science.288.5465.505 · PubMed

Other PDB entries of the same protein (UniProt P04228 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6BLQ 1.8 Å, Crystal Structure of IAg7 in complex with insulin mimotope p8E9E
7QHP 1.82 Å, Structure of I-Ag7 with a bound hybrid insulin peptide
6BLR 1.96 Å, Crystal Structure of IAg7 in complex with insulin mimotope p8E9E6SS
6BLX 2.32 Å, Crystal structure of IAg7 in complex with insulin mimotope p8G9E
2IAD 2.4 Å, Class II MHC I-ad in complex with an influenza hemagglutinin peptide 126-138
5DMK 2.45 Å, Crystal Structure of IAg7 in complex with RLGL-WE14
1IAO 2.6 Å, Class II MHC I-ad in complex with ovalbumin peptide 323-339
7Z50 2.65 Å, Structure of the highly diabetogenic 4.1-T cell receptor targeting a hybrid insulin…
3MBE 2.89 Å, TCR 21.30 in complex with MHC class II I-Ag7HEL(11-27)
7RDV 2.9 Å, TFH TCR bound to MHC Class II IAd presenting aggrecan epitope
3CUP 3.09 Å, Crystal structure of the MHC class II molecule I-Ag7 in complex with the peptide…
1F3J 3.1 Å, Histocompatibility antigen I-AG7

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