2IAD: Class II MHC I-ad

Class II MHC I-ad in complex with an influenza hemagglutinin peptide 126-138. Determined by X-ray diffraction at 2.4 Å resolution. Released 18 Nov 1998.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Mus musculus
Chains: 2
Atoms: 3,243
Mol. weight: 45.71 kDa
Released: 18 Nov 1998

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

Secondary structure: helices and β-sheets

2IAD contains 12 α-helices and 29 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: 2 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	4-14	11	1
β-strand	19-26	8	1
β-strand	29-35	7	1
β-strand	40-43	4	1
α-helix	57-77	21
α-helix	80-82	3
β-strand	88-93	6	2
β-strand	103-112	10	2
β-strand	118-123	6	3
β-strand	126-127	2	3
β-strand	132-134	3	2
β-strand	138-139	2	2
β-strand	145-153	9	2
β-strand	160-166	7	3
β-strand	174-179	10	3

Chain B: 10 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	131P-135P	5
β-strand	8-18	11	1
β-strand	23-32	10	1
β-strand	35-41	7	1
β-strand	47-49	3	1
α-helix	52-54	3
α-helix	55-63	9
α-helix	65-74	10
α-helix	75-80	6
α-helix	81-82	2
α-helix	83-87	5
α-helix	88-89	2
α-helix	91-93	3
β-strand	95	1	4
β-strand	98-103	6	5
β-strand	115-122	8	5
β-strand	123	1	4
β-strand	128-133	6	6
β-strand	136-138	3	6
β-strand	142-144	3	5
α-helix	145-147	3
β-strand	148-149	2	5
β-strand	155-161	7	5
β-strand	171-176	6	6
β-strand	184	1	6
β-strand	187-188	2	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
MHC class II I-ad	A	protein	194	Mus musculus	P04228 (AlphaFold model)
MHC class II I-ad	B	protein	205	Mus musculus	P01921 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2IAD_1 MHC CLASS II I-AD (chains A)
EDDIEADHVGFYGTTVYQSPGDIGQYTHEFDGDELFYVDLDKKKTVWRLPEFGQLILFEP
QGGLQNIAAEKHNLGILTKRSNFTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPV
INITWLRNSKSVTDGVYETSFLVNRDHSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLK
HWEPEISSADLVPR

Sequence of entity 2 (B), FASTA

>2IAD_2 MHC CLASS II I-AD (chains B)
GHATQGVTAASSHEGNSERHFVVQFKGECYYTNGTQRIRLVTRYIYNREEYVRYDSDVGE
YRAVTELGRPDAEYWNSQPEILERTRAEVDTACRHNYEGPETSTSLRRLEQPNVAISLSR
TEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLIRNGDWTFQVLVMLEMTP
HQGEVYTCHVEHPSLKSPITVEWSS

Primary citation

Crystal structures of two I-Ad-peptide complexes reveal that high affinity can be achieved without large anchor residues. Scott, C.A., Peterson, P.A., Teyton, L. et al. Immunity (1998) 8:319-329. DOI 10.1016/S1074-7613(00)80537-3 · 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
5DMK 2.45 Å, Crystal Structure of IAg7 in complex with RLGL-WE14
1ES0 2.6 Å, Crystal structure of the murine class II allele I-A(G7) complexed with the glutamic acid…
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

Browse structure collections

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