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Magnesium in PDB 1ky3: Gdp-Bound YPT7P at 1.35 A Resolution

Protein crystallography data

The structure of Gdp-Bound YPT7P at 1.35 A Resolution, PDB code: 1ky3 was solved by A.-T.Constantinescu, A.Rak, A.J.Scheidig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.61 / 1.35
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 49.535, 55.430, 60.177, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 23.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Gdp-Bound YPT7P at 1.35 A Resolution (pdb code 1ky3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Gdp-Bound YPT7P at 1.35 A Resolution, PDB code: 1ky3:

Magnesium binding site 1 out of 1 in 1ky3

Go back to Magnesium Binding Sites List in 1ky3
Magnesium binding site 1 out of 1 in the Gdp-Bound YPT7P at 1.35 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Gdp-Bound YPT7P at 1.35 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:24.0
occ:1.00
O3B A:GDP400 2.0 21.8 1.0
O A:HOH586 2.0 24.4 1.0
O A:HOH583 2.1 24.9 1.0
OG1 A:THR22 2.1 23.5 1.0
O A:HOH585 2.2 28.6 1.0
O A:HOH584 2.2 24.0 1.0
CB A:THR22 3.2 21.0 1.0
PB A:GDP400 3.2 21.9 1.0
O2B A:GDP400 3.5 24.5 1.0
N A:THR22 3.9 18.7 1.0
OD1 A:ASP64 4.0 27.0 1.0
CA A:THR22 4.1 19.2 1.0
OD2 A:ASP64 4.2 26.6 1.0
O1A A:GDP400 4.2 25.2 1.0
CG2 A:THR22 4.2 25.0 1.0
O1B A:GDP400 4.3 20.2 1.0
O3A A:GDP400 4.3 20.8 1.0
O A:HOH617 4.4 38.5 1.0
CG A:ASP64 4.5 26.0 1.0
PA A:GDP400 4.6 21.5 1.0
O2A A:GDP400 4.8 22.2 1.0
O A:HOH551 4.8 28.1 1.0
CB A:LYS21 4.9 19.2 1.0
NZ A:LYS21 4.9 21.1 1.0
OG1 A:THR65 4.9 53.0 1.0
O A:HOH618 4.9 44.0 1.0
O A:HOH553 5.0 35.2 1.0
CE A:LYS21 5.0 20.7 1.0

Reference:

A.T.Constantinescu, A.Rak, K.Alexandrov, H.Esters, R.S.Goody, A.J.Scheidig. Rab-Subfamily-Specific Regions of YPT7P Are Structurally Different From Other Rabgtpases. Structure V. 10 569 2002.
ISSN: ISSN 0969-2126
PubMed: 11937061
DOI: 10.1016/S0969-2126(02)00737-2
Page generated: Tue Aug 13 08:11:31 2024

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