5E6X: Integrin beta-2

Re-refinement of the Crystal Structure of the Plexin-Semaphorin-Integrin Domain/Hybrid Domain/I-EGF1 Segment from the Human Integrin b2 Subunit. Determined by X-ray diffraction at 1.75 Å resolution. Released 2 Mar 2016.

Method
X-ray diffraction
Resolution
1.75 Å
Organism
Homo sapiens
Chains
1
Atoms
2,517
Mol. weight
31.72 kDa
Ligands
NAG
Released
2 Mar 2016

Explore 5E6X in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5E6X contains 11 α-helices and 24 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: 11 helices, 24 β-strands

ElementResiduesLengthSheet
α-helix11-155
β-strand22-2431
α-helix36-394
β-strand40-4121
α-helix43-486
α-helix53-553
β-strand56-5721
β-strand62-6652
β-strand76-7723
β-strand80-8562
β-strand91-9773
β-strand9914
β-strand345-34952
β-strand356-36383
β-strand369-37353
β-strand376-37832
β-strand38314
β-strand387-39593
α-helix399-4013
β-strand402-40872
β-strand415-42172
α-helix436-4394
β-strand441-44445
β-strand447-45045
α-helix4511
β-strand454-45526
β-strand461-46226
α-helix468-4736
α-helix4821
α-helix483-4864
β-strand488-49147
β-strand494-49747
α-helix498-4992
β-strand506-50838
β-strand514-51638

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Integrin beta-2Aprotein280Homo sapiensP05107 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5E6X_1 Integrin beta-2 (chains A)
QECTKFKVSSCRECIESGPGCTWCQKLNFTGPGDPDSIRCDTRPQLLMRGCAADDIMDPT
SLAETQEDHNGGQKQLSPQKVTLYLRPGQAAAFNVTFRRAKLSSRVFLDHNALPDTLKVT
YDSFCSNGVTHRNQPRGDCDGVQINVPITFQVKVTATECIQEQSFVIRALGFTDIVTVQV
LPQCECRCRDQSRDRSLCHGKGFLECGICRCDTGYIGKNCECQTQGRSSQELEGSCRKDN
NSIICSGLGDCVCGQCLCHTSDVPGKLIYGQYCEHHHHHH

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O63

Primary citation

Leukocyte integrin alpha L beta 2 headpiece structures: The alpha I domain, the pocket for the internal ligand, and concerted movements of its loops. Sen, M., Springer, T.A. Proc Natl Acad Sci U S A (2016) 113:2940-2945. DOI 10.1073/pnas.1601379113 · PubMed

Other PDB entries of the same protein (UniProt P05107 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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