Brand  (β version)

PDB ID: 5O74

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Ligands
Code Name Style Show Link
GDP Guanosine-5'-diphosphate PoSSuM
Non-standard Residues
Code Name Show
9MN (2~{S})-2-azanyl-6-(6-bromanylhexanoylamino)hexanoic acid
Glycosylation
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Structure summary

Code : 5O74   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Crystal structure of human Rab1b covalently bound to the GEF domain of DrrA/SidM from Legionella pneumophila in the presence of GDP
Release Data : 2017-10-11
Compound :
mol_id molecule chains synonym
1 Multifunctional virulence effector protein DrrA A,C,E,G,I,K Defects in Rab1 recruitment protein A
ec: 2.7.7.-
mutation: D512C
mol_id molecule chains
2 Ras-related protein Rab-1B B,D,F,H,J,L
Source :
mol_id organism_scientific expression_system
1 Legionella pneumophila  (taxid:446) Escherichia coli  (taxid:562)
gene: drrA, sidM
mol_id organism_scientific organism_common expression_system
2 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: RAB1B
Authors : Cigler, M., Mueller, T., Horn-Ghetko, D., von Wrisberg, M.K., Fottner, M., Goody, R.S., Itzen, A., Mueller, M.P., Lang, K.
Keywords : Rab1b, DrrA, exchange factor, Legionella pneumophila, hydrolase
Exp. method : X-RAY DIFFRACTION ( 2.500 Å )
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.
(2017)  Angew. Chem. Int. Ed. Engl.  56 : 15737 - 15741

PubMed: 28960788
DOI: 10.1002/anie.201706927

Reaction

Chain : A, C, E, G, I, K
UniProt : Q29ST3 (DRRA_LEGPN)
Reaction: EC: Evidence:
Physiological Direction:
ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L- tyrosyl-[protein] 2.7.7.108 PubMed:20651120
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ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl- [protein] + diphosphate 2.7.7.108 PubMed:20651120
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GTP + L-tyrosyl-[protein] = diphosphate + O-(5'-guanylyl)-L- tyrosyl-[protein] 2.7.7.n6 PubMed:20651120
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Chain : B, D, F, H, J, L
UniProt : Q9H0U4 (RAB1B_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
GTP + H2O = GDP + H(+) + phosphate 3.6.5.2 UniProtKB:P62820
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