2.5.1.60: protein geranylgeranyltransferase type II

This is an abbreviated version!
For detailed information about protein geranylgeranyltransferase type II, go to the full flat file.

Reaction

Synonyms

AtRGTA1, AtRGTA2, AtRGTB1, Chm, geranylgeranyl transferase type I subunit alpha 1, geranylgeranyl transferase type I subunit alpha 2, geranylgeranyl transferase type II subunit beta 1, geranylgeranyl transferase type II subunit beta 2, geranylgeranyl transferase type-1 subunit alpha 1, geranylgeranyl transferase type-2 subunit alpha 2, geranylgeranyl transferase type-2 subunit beta 1, geranylgeranyl transferase type-2 subunit beta 2, geranylgeranyltransferase II, geranylgeranyltransferase type II, GGT2, GGTase-II, GGTase3, GGTaseII, PGGT-II, protein geranylgeranyltransferase type-II, PTAR1, Rab geranylgeranyl transferase, Rab geranylgeranyl transferase alpha subunit 2, Rab geranylgeranyl transferase beta subunit 1, Rab geranylgeranyl transferase beta subunit 2, Rab geranylgeranyl transferase lpha subunit 1, Rab geranylgeranyl-transferase, Rab geranylgeranyltransferase, Rab geranylgeranyltransferase type II, Rab GG transferase, Rab GGTase, Rab proteins geranylgeranyltransferase component A 1, RAB-GGT, Rab-GGT alpha 1, Rab-GGT alpha 2, Rab-GGT beta 1, Rab-GGT beta 2, Rab11a, RabGGT, RabGGTase, Rabggtb, REP/GGTase, RGGT, RGT alphabeta, RGTA1, RGTA2, RGTB1, RGTB2

ECTree

     2 Transferases

         2.5 Transferring alkyl or aryl groups, other than methyl groups

             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)

                2.5.1.60 protein geranylgeranyltransferase type II

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Results	in table
8	Activating Compound
6396	AA Sequence
3	Application
1	CAS Registry Number
18	Cloned(Commentary)
2	Cofactor
6	Crystallization (Commentary)
280	Disease/ Diagnostics
2	Expression
16	General Information
32	IC50 Value
89	Inhibitors
10	Ki Value [mM]
9	KM Value [mM]
2	Localization
5	Metals/Ions
6	Molecular Weight [Da]
21	Natural Substrates/ Products (Substrates)
55	Organism
43	PDB ID
2	pH Optimum
6	Protein Variants
11	Purification (Commentary)
19	Reaction
50	Reference
24	Source Tissue
4	Specific Activity [micromol/min/mg]
79	Substrates and Products (Substrate)
10	Subunits
100	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
2	Turnover Number [1/s]

Crystallization

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of the Enzyme Summary Page.

Crystallization on EC 2.5.1.60 - protein geranylgeranyltransferase type II

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

enzyme-inhibitor complex with an engeneered enzyme lacking the LRR- and Ig-domains, complexes are prepared by soaking of co-crystallization, diffraction data collection at -173°C

Homo sapiens

-

709461

structure of the full-length GGTase3-FBXL2-SKP1 complex reveals an extensive multivalent interface specifically formed between the leucine-rich repeat domain of substrate FBXL2 and subunit PTAR1

Homo sapiens

P53611; Q7Z6K3

759843

-

Rattus norvegicus

-

638594

at 2.0 Angstrom resolution, the beta subunit forms an alpha-alpha barrel that contains most of the residues in the active site, the alpha subunit consists of a helical domain, an immunoglobulin-like domain and a leucine-rich repeat domain, the N-terminal alpha subunit binds to the active site in the beta subunit

Rattus norvegicus

-

638589

at 2.7 Angstom, crystal structure of REP-1 in complex with farnesyl-loaded enzyme, contact between the two proteins is formed through domain II of REP-1 and the alpha subunit of the enzyme

Rattus norvegicus

-

638596

in complex with geranylgeranyl diphosphate, hanging drop vapour diffusion method, with 14% (w/v) PEG 3350, 0.2M CaAc2, 0.1 M HEPES pH 7.2

Rattus norvegicus

-

686394