1M1U: Integrin alpha-M

An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11B a-domain. Determined by X-ray diffraction at 2.3 Å resolution. Released 7 Aug 2002.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
Homo sapiens
Chains
1
Atoms
1,530
Mol. weight
22.3 kDa
Ligands
CA
Released
7 Aug 2002

Explore 1M1U in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1M1U contains 13 α-helices and 8 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: 13 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand133-14081
α-helix147-16317
β-strand169-17681
β-strand180-18451
α-helix186-1916
α-helix195-1995
β-strand20912
α-helix211-2177
α-helix218-2225
α-helix225-2273
β-strand234-24181
β-strand246-24722
α-helix252-2543
α-helix256-2616
β-strand264-27071
α-helix278-28710
α-helix2891
α-helix292-2943
β-strand296-29831
α-helix304-3118
α-helix312-3143

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Integrin alpha-MAprotein195Homo sapiensP11215 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1M1U_1 Integrin alpha-M (chains A)
GSEALRGSPQEDSDIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKSKTLFSLMQYSEEF
RIHFTFKEFQNNPNPRSLVKPITQLLGRTHTATGIRKVVRELFNITNGARKNAFKILVVI
TDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDAFRSEKSRQELNTIASKPPRDHVFQVN
NFEALKTIQNQLREK

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa1

Primary citation

An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domain. Xiong, J.P., Li, R., Essafi, M. et al. J Biol Chem (2000) 275:38762-38767. DOI 10.1074/jbc.C000563200 · PubMed

Other PDB entries of the same protein (UniProt P11215 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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