5O74: Human Rab1b covalently

Crystal structure of human Rab1b covalently bound to the GEF domain of DrrA/SidM from Legionella pneumophila in the presence of GDP. Determined by X-ray diffraction at 2.5 Å resolution. Released 11 Oct 2017.

Method
X-ray diffraction
Resolution
2.5 Å
Organisms
Legionella pneumophila, Homo sapiens
Chains
12
Atoms
17,004
Mol. weight
258.3 kDa
Ligands
GDP
Released
11 Oct 2017

Explore 5O74 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5O74 contains 107 α-helices and 66 β-strands across 12 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: 12 helices, 3 β-strands

ElementResiduesLengthSheet
α-helix343-36119
α-helix365-38218
α-helix386-3894
α-helix390-3934
α-helix400-41920
α-helix428-44720
α-helix452-4543
α-helix458-4603
α-helix461-4633
α-helix464-47815
β-strand484-48521
β-strand488-48921
α-helix490-50617
α-helix512-5209
β-strand52812
Chain B: 9 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand7-1483
α-helix21-244
α-helix25-273
β-strand2913
α-helix30-323
α-helix36-416
β-strand45-5283
β-strand55-6283
α-helix67-693
α-helix75-773
β-strand83-8973
α-helix93-10917
β-strand115-12173
α-helix133-14210
β-strand147-15043
β-strand15114
β-strand15614
α-helix158-17215
Chain C: 10 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix342-36120
α-helix365-38218
α-helix386-3894
α-helix390-3934
α-helix400-41920
α-helix428-44720
α-helix452-4543
α-helix464-47815
β-strand484-48525
β-strand488-48925
α-helix490-50617
α-helix512-5209
Chain D: 7 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand7-1486
α-helix21-244
β-strand2916
α-helix30-323
α-helix36-416
β-strand45-5286
β-strand55-6286
α-helix67-693
β-strand83-8976
α-helix93-10816
β-strand115-12176
α-helix133-14311
β-strand147-15046
β-strand15117
β-strand15617
α-helix158-17215
Chain E: 10 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix343-36119
α-helix365-38218
α-helix386-3894
α-helix390-3934
α-helix400-41920
α-helix428-44720
α-helix452-4543
α-helix464-47815
β-strand484-48528
β-strand488-48928
α-helix490-50617
α-helix512-5209
Chain F: 7 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand7-1489
α-helix21-288
α-helix37-415
β-strand45-5289
β-strand55-6289
α-helix67-693
α-helix75-773
β-strand83-8979
α-helix93-10917
β-strand115-12179
α-helix133-14311
β-strand147-15049
β-strand151110
β-strand156110
α-helix158-17215
Chain G: 10 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix342-36120
α-helix365-38117
α-helix386-3894
α-helix390-3934
α-helix400-41920
α-helix428-44720
α-helix452-4543
α-helix464-47815
β-strand484-485211
β-strand488-489211
α-helix490-50617
α-helix512-5209
β-strand52813
Chain H: 8 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand7-1482
α-helix21-244
α-helix25-273
β-strand2912
α-helix36-416
β-strand45-5282
β-strand55-6282
α-helix67-693
α-helix75-784
β-strand83-8972
α-helix93-10917
β-strand115-12172
α-helix133-14210
β-strand147-15042
β-strand151112
β-strand156112
α-helix158-17215

3 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Multifunctional virulence effector protein DrrAA, C, E, G, I, Kprotein197Legionella pneumophilaQ29ST3 (AlphaFold model)
Ras-related protein Rab-1BB, D, F, H, J, Lprotein180Homo sapiensQ9H0U4 (AlphaFold model)
Sequence of entity 1 (A, C, E, G, I, K), FASTA
>5O74_1 Multifunctional virulence effector protein DrrA (chains A, C, E, G, I, K)
GHMVTRIENLENAKKLWDNANSMLEKGNISGYLKAANELHKFMKEKNLKEDDLRPELSDK
TISPKGYAILQSLWGAASDYSRAAATLTESTVEPGLVSAVNKMSAFFMDCKLSPNERATP
DPDFKVGKSKILVGIMQFIKDVADPTSKIWMHNTKALMNHKIAAIQKLERSNNVNCETLE
SVLSSKGENLSEYLSYK
Sequence of entity 2 (B, D, F, H, J, L), FASTA
>5O74_2 Ras-related protein Rab-1B (chains B, D, F, H, J, L)
MAPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQ
IWDTAGQERFRTITSSYYXGAHGIIVVYDVTDQESYANVKQWLQEIDRYASENVNKLLVG
NKSDLTTKKVVDNTTAKEFADSLGIPFLETSAKNATNVEQAFMTMAAEIKKRMGHHHHHH

Ligands and cofactors

IDNameFormulaCopies
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P26

Primary citation

Proximity-Triggered Covalent Stabilization of Low-Affinity Protein Complexes In Vitro and In Vivo. Cigler, M., Muller, T.G., Horn-Ghetko, D. et al. Angew Chem Int Ed Engl (2017) 56:15737-15741. DOI 10.1002/anie.201706927 · PubMed

Other PDB entries of the same protein (UniProt Q29ST3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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