4XW2: Integrin alpha-M

Structural basis for simvastatin competitive antagonism of complement receptor 3. Determined by X-ray diffraction at 2.0 Å resolution. Released 13 Jan 2016.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
1
Atoms
1,587
Mol. weight
22.94 kDa
Ligands
SIM, MG
Released
13 Jan 2016

Explore 4XW2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4XW2 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
α-helix2331
β-strand234-24181
β-strand24612
α-helix252-2543
α-helix256-2616
β-strand265-27061
α-helix278-28710
α-helix2891
α-helix292-2943
β-strand296-29831
α-helix303-31412

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Integrin alpha-MAprotein198Homo sapiensP11215 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4XW2_1 Integrin alpha-M (chains A)
GAMGSPQEDSDIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKSKTLFSLMQYSEEFRIH
FTFKEFQNNPNPRSLVKPITQLLGRTHTATGIRKVVRELFNITNGARKNAFKILVVITDG
EKFGDPLGYEDVIPEADREGVIRYVIGVGDAFRSEKSRQELNTIASKPPRDHVFQVNNFE
ALKTIQNQLREKGFAIEG

Ligands and cofactors

IDNameFormulaCopies
SIMSimvastatin acidC25 H40 O61
MGMagnesium ionMg1

Primary citation

Structural Basis for Simvastatin Competitive Antagonism of Complement Receptor 3. Jensen, M.R., Bajic, G., Zhang, X. et al. J Biol Chem (2016) 291:16963-16976. DOI 10.1074/jbc.M116.732222 · 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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