1IAK: Histocompatibility antigen I-ak

Name: PDB 1IAK: Histocompatibility antigen I-ak
Published: 1998-04-15
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: histocompatibility antigen i-ak

Histocompatibility antigen I-ak. Determined by X-ray diffraction at 1.9 Å resolution. Released 15 Apr 1998.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Mus musculus
Chains: 3
Atoms: 3,540
Mol. weight: 46.79 kDa
Ligands: NAG
Released: 15 Apr 1998

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

Secondary structure: helices and β-sheets

1IAK contains 17 α-helices and 30 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: 4 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	5-15	12	1
β-strand	19-26	8	1
β-strand	29-35	7	1
β-strand	40-43	4	1
α-helix	46-50	5
β-strand	53	1	2
α-helix	56-77	22
α-helix	80-84	5
β-strand	88-93	6	3
β-strand	103-112	10	3
β-strand	118-123	6	4
β-strand	126-127	2	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	161-166	6	4
β-strand	174-178	5	4

Chain B: 12 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	7-18	12	1
α-helix	20-22	3
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	55-64	10
α-helix	68-72	5
α-helix	74	1
α-helix	75-80	6
α-helix	81-82	2
α-helix	83-86	5
α-helix	90-92	3
β-strand	95	1	5
α-helix	96-97	2
β-strand	98-103	6	6
α-helix	106-107	2
β-strand	113-122	10	6
β-strand	123	1	5
β-strand	128-133	6	7
β-strand	136-138	3	7
β-strand	142-144	3	6
α-helix	146-147	2
β-strand	148-149	2	6
β-strand	155-163	9	6
β-strand	170-176	7	7
β-strand	184-189	6	7

Chain P: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
β-strand	51	1	2
α-helix	54-61	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
MHC class II I-ak	A	protein	199	Mus musculus	P01910 (AlphaFold model)
MHC class II I-ak	B	protein	185	Mus musculus	P06343 (AlphaFold model)
MHC class II I-ak	P	protein	13	Mus musculus	Q29431 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1IAK_1 MHC CLASS II I-AK (chains A)
EDDIEADHVGSYGITVYQSPGDIGQYTFEFDGDELFYVDLDKKETVWMLPEFAQLRRFEP
QGGLQNIATGKHNLEILTKRSNSTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPV
INITWLRNSKSVTDGVYETSFFVNRDYSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLK
HWEPEIPAPMSELTETVVC

Sequence of entity 2 (B), FASTA

>1IAK_2 MHC CLASS II I-AK (chains B)
GSFVHQFQPFCYFTNGTQRIRLVIRYIYNREEYVRFDSDVGEYRAVTELGRPDAEYWNKQ
YLERTRAELDTVCRHNYEKTETPTSLRRLEQPSVVISLSRTEALNHHNTLVCSVTDFYPA
KIKVRWFRNGQEETVGVSSTQLIRNGDWTFQVLVMLEMTPRRGEVYTCHVEHPSLTSPIT
VEWRA

Sequence of entity 3 (P), FASTA

>1IAK_3 MHC CLASS II I-AK (chains P)
STDYGILQINSRW

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	3

Primary citation

Crystal structure of I-Ak in complex with a dominant epitope of lysozyme. Fremont, D.H., Monnaie, D., Nelson, C.A. et al. Immunity (1998) 8:305-317. DOI 10.1016/S1074-7613(00)80536-1 · PubMed

Other PDB entries of the same protein (UniProt P01910 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9L1L 3.09 Å, Structure of anti-HEL AiTab
1D9K 3.2 Å, Crystal structure of complex between D10 TCR and pmhc I-ak/ca
1JL4 4.3 Å, Crystal structure of the human CD4 N-terminal two domain fragment complexed to a class…

Browse structure collections

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