8D4V: Cathepsin G Inhibited by Eap2 from S. aureus

Crystal Structure of Cathepsin G Inhibited by Eap2 from S. aureus. Determined by X-ray diffraction at 1.85 Å resolution. Released 21 Dec 2022.

Method
X-ray diffraction
Resolution
1.85 Å
Organisms
Homo sapiens, Staphylococcus aureus subsp. aureus Mu50
Chains
4
Atoms
5,312
Mol. weight
73.03 kDa
Released
21 Dec 2022

Explore 8D4V in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8D4V contains 26 α-helices and 64 β-strands across 4 chains. 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: 10 helices, 22 β-strands

ElementResiduesLengthSheet
β-strand1711
β-strand20-2122
α-helix22-232
β-strand30-3673
β-strand41-50103
β-strand53-5643
α-helix58-603
β-strand64-6963
β-strand7314
β-strand82-91103
β-strand9615
β-strand10115
β-strand105-10953
α-helix112-1154
β-strand11616
β-strand11916
β-strand12312
α-helix124-1252
β-strand136-14162
β-strand15314
β-strand155-16172
α-helix162-1632
α-helix165-1684
β-strand179-18242
β-strand19011
β-strand199-20242
β-strand205-21392
α-helix2181
α-helix2201
β-strand221-22552
α-helix226-2294
α-helix230-2378
Chain B: 3 helices, 10 β-strands
ElementResiduesLengthSheet
β-strand158-16583
β-strand166113
β-strand169113
β-strand170-17122
β-strand174-17963
β-strand184-186314
α-helix187-20216
α-helix206-2116
β-strand216-22163
β-strand226-23053
β-strand240-242314
α-helix243-2453
β-strand246-25273
Chain C: 10 helices, 22 β-strands
ElementResiduesLengthSheet
β-strand1717
β-strand20-2128
α-helix22-232
β-strand30-3679
β-strand41-50109
β-strand53-5649
α-helix58-603
β-strand64-6969
β-strand73110
β-strand82-91109
β-strand96111
β-strand101111
β-strand105-10959
α-helix112-1154
β-strand116112
β-strand119112
β-strand12318
α-helix124-1252
β-strand136-14168
β-strand153110
β-strand155-16178
α-helix162-1632
α-helix164-1685
β-strand179-18248
β-strand19017
β-strand199-20248
β-strand205-21398
α-helix2181
α-helix2201
β-strand221-22558
α-helix226-2294
α-helix230-2378
Chain D: 3 helices, 10 β-strands
ElementResiduesLengthSheet
β-strand157-16599
β-strand166115
β-strand169115
β-strand170-17128
β-strand174-18079
β-strand184-186316
α-helix187-20216
α-helix206-2116
β-strand216-22169
β-strand226-23059
β-strand240-242316
α-helix243-2453
β-strand246-25279

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cathepsin G, C-terminal truncated formA, Cprotein223Homo sapiensP08311 (AlphaFold model)
Extracellular Adherence ProteinB, Dprotein100Staphylococcus aureus subsp. aureus Mu50Q99QS1 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>8D4V_1 Cathepsin G, C-terminal truncated form (chains A, C)
IIGGRESRPHSRPYMAYLQIQSPAGQSRCGGFLVREDFVLTAAHCWGSNINVTLGAHNIQ
RRENTQQHITARRAIRHPQYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGT
LCTVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIFGSYDPRRQICVGDRRERKAAFKGD
SGGPLLCNNVAHGIVSYGKSSGVPPEVFTRVSSFLPWIRTTMR
Sequence of entity 2 (B, D), FASTA
>8D4V_2 Extracellular Adherence Protein (chains B, D)
GSTVQVPYTITVNGTSQNILSNLTFNKNQNISYKDLEGKVKSVLESNRGITDVDLRLSKQ
AKYTVNFKNGTKKVIDLKSGIYTANLINSSDIKSININVD

Primary citation

Characterization of two distinct neutrophil serine protease-binding modes within a Staphylococcus aureus innate immune evasion protein family. Gido, C.D., Herdendorf, T.J., Geisbrecht, B.V. J Biol Chem (2023) 299:102969-102969. DOI 10.1016/j.jbc.2023.102969 · PubMed

Other PDB entries of the same protein (UniProt P08311 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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