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Zinc in PDB 4gtm: Ftase in Complex with Bms Analogue 11

Enzymatic activity of Ftase in Complex with Bms Analogue 11

All present enzymatic activity of Ftase in Complex with Bms Analogue 11:
2.5.1.58; 2.5.1.59;

Protein crystallography data

The structure of Ftase in Complex with Bms Analogue 11, PDB code: 4gtm was solved by Z.Guo, E.A.Stigter, R.S.Bon, H.Waldmann, W.Blankenfeldt, R.S.Goody, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.94 / 2.20
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 173.171, 173.171, 70.289, 90.00, 90.00, 120.00
R / Rfree (%) 17.3 / 21.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Ftase in Complex with Bms Analogue 11 (pdb code 4gtm). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Ftase in Complex with Bms Analogue 11, PDB code: 4gtm:

Zinc binding site 1 out of 1 in 4gtm

Go back to Zinc Binding Sites List in 4gtm
Zinc binding site 1 out of 1 in the Ftase in Complex with Bms Analogue 11


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Ftase in Complex with Bms Analogue 11 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn501

b:27.7
occ:1.00
NE2 B:HIS362 2.1 23.9 1.0
NBE B:7TM503 2.1 40.3 1.0
OD2 B:ASP297 2.2 19.9 1.0
OD1 B:ASP297 2.3 19.4 1.0
SG B:CYS299 2.4 21.7 1.0
CG B:ASP297 2.6 21.0 1.0
CAT B:7TM503 3.0 43.0 1.0
CE1 B:HIS362 3.0 22.2 1.0
CD2 B:HIS362 3.1 21.7 1.0
CAS B:7TM503 3.2 37.1 1.0
CB B:CYS299 3.4 19.9 1.0
N B:CYS299 4.0 20.7 1.0
CB B:ASP297 4.0 21.8 1.0
ND1 B:HIS362 4.1 21.3 1.0
NBU B:7TM503 4.1 45.6 1.0
CE2 B:TYR361 4.2 20.6 1.0
CG B:HIS362 4.2 20.3 1.0
C1 B:DMS504 4.2 68.5 1.0
CA B:CYS299 4.3 20.5 1.0
CBP B:7TM503 4.3 38.8 1.0
CB B:ASP352 4.3 24.7 1.0
CG B:ASP352 4.3 24.4 1.0
OD2 B:ASP352 4.4 27.9 1.0
C2 B:DMS504 4.5 66.0 1.0
O B:HOH624 4.6 27.9 1.0
CA B:ASP352 4.7 24.8 1.0
CD2 B:TYR361 4.8 22.0 1.0
OD1 B:ASP352 4.9 25.1 1.0
N B:GLY298 4.9 21.4 1.0
OH B:TYR361 5.0 24.1 1.0
C B:ASP297 5.0 22.2 1.0

Reference:

E.A.Stigter, Z.Guo, R.S.Bon, Y.W.Wu, A.Choidas, A.Wolf, S.Menninger, H.Waldmann, W.Blankenfeldt, R.S.Goody. Development of Selective, Potent Rabggtase Inhibitors J.Med.Chem. V. 55 8330 2012.
ISSN: ISSN 0022-2623
PubMed: 22963166
DOI: 10.1021/JM300624S
Page generated: Sat Oct 26 23:30:43 2024

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