1IAM: Intercellular adhesion molecule-1

Structure of the two amino-terminal domains of human intercellular adhesion molecule-1, icam-1. Determined by X-ray diffraction at 2.1 Å resolution. Released 29 Apr 1998.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,597
Mol. weight: 20.7 kDa
Ligands: NAG
Released: 29 Apr 1998

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

Secondary structure: helices and β-sheets

1IAM contains 3 α-helices and 22 β-strands across 1 chain. 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: 3 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	2-5	4	1
β-strand	8-12	5	2
β-strand	15-23	9	1
β-strand	30-34	5	3
β-strand	39-42	4	1
β-strand	49-57	9	1
β-strand	61	1	2
β-strand	64-68	5	3
β-strand	73-77	5	3
β-strand	79-83	5	2
β-strand	84	1	4
β-strand	88-91	4	5
α-helix	92-93	2
β-strand	97-98	2	6
β-strand	103-111	9	5
β-strand	114	1	4
α-helix	116-118	3
β-strand	119-125	7	7
β-strand	128-134	7	7
β-strand	140-147	8	5
β-strand	156-164	9	7
α-helix	166-168	3
β-strand	172-176	5	7
β-strand	180-181	2	7
β-strand	183-184	2	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Intercellular adhesion molecule-1	A	protein	185	Homo sapiens	P05362 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1IAM_1 INTERCELLULAR ADHESION MOLECULE-1 (chains A)
QTSVSPSKVILPRGGSVLVTCSTSCDQPKLLGIETPLPKKELLLPGNNRKVYELSNVQED
SQPMCYSNCPDGQSTAKTFLTVYWTPERVELAPLPSWQPVGKQLTLRCQVEGGAPRAQLT
VVLLRGEKELKREPAVGEPAEVTTTVLVRRDHHGAQFSCRTELDLRPQGLELFENTSAPY
QLQTF

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1

Primary citation

The structure of the two amino-terminal domains of human ICAM-1 suggests how it functions as a rhinovirus receptor and as an LFA-1 integrin ligand. Bella, J., Kolatkar, P.R., Marlor, C.W. et al. Proc Natl Acad Sci U S A (1998) 95:4140-4145. DOI 10.1073/pnas.95.8.4140 · PubMed

Other PDB entries of the same protein (UniProt P05362 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7BG7 2.4 Å, HRV14 in complex with its receptor ICAM-1
2OZ4 2.7 Å, Structural Plasticity in IgSF Domain 4 of ICAM-1 Mediates Cell Surface Dimerization
5MZA 2.78 Å, The DBLb domain of PF11_0521 PfEMP1 bound to human ICAM-1
1IC1 3.0 Å, The crystal structure for the N-terminal two domains of icam-1
1P53 3.06 Å, The Crystal Structure of ICAM-1 D3-D5 fragment
1D3L 3.25 Å, D1D2-icam-1 fully glycosylated, variation of D1-D2 interdomain angle in different…
1MQ8 3.3 Å, Crystal structure of alphaL I domain in complex with ICAM-1
3TCX 3.6 Å, Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain…
6S8U 3.67 Å, Structure of the PfEMP1 IT4var13 DBLbeta domain bound to ICAM-1
6EIT 3.9 Å, Coxsackievirus A24v in complex with the D1-D2 fragment of ICAM-1
1Z7Z 8.0 Å, Cryo-em structure of human coxsackievirus A21 complexed with five domain icam-1kilifi
1D3I 26.0 Å, cryo-EM structure of human rhinovirus 14 (HRV14) complexed with a two-domain fragment of…

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