1IAM

STRUCTURE OF THE TWO AMINO-TERMINAL DOMAINS OF HUMAN INTERCELLULAR ADHESION MOLECULE-1, ICAM-1

Summary for 1IAM

DescriptorINTERCELLULAR ADHESION MOLECULE-1, N-ACETYL-D-GLUCOSAMINE (3 entities in total)
Functional Keywordsrhinovirus receptor, cell adhesion, integrin ligand, glycoprotein, lfa-1 ligand, immunoglobulin fold, transmembrane, viral protein receptor
Biological sourceHomo sapiens (human)
Cellular locationMembrane; Single-pass type I membrane protein P05362
Total number of polymer chains1
Total molecular weight20701.55
Authors
Bella, J.,Kolatkar, P.R.,Marlor, C.,Greve, J.M.,Rossmann, M.G. (deposition date: 1998-02-22, release date: 1998-04-29, Last modification date: 2011-11-16)
Primary citation
Bella, J.,Kolatkar, P.R.,Marlor, C.W.,Greve, J.M.,Rossmann, M.G.
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.
Proc.Natl.Acad.Sci.USA, 95:4140-4145, 1998
PubMed: 9539703 (PDB entries with the same primary citation)
DOI: 10.1073/pnas.95.8.4140
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.1 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers160.5%9.1%8.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

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More Biological unit images

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(*)In the case of coarse surface representation, the asymmetric unit is shown as red ribbon representation.
Coordinate files for Biological unit (1iam.pdb1.gz [66.35 KB])