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Magnesium in PDB 1xmj: Crystal Structure of Human DELTAF508 Human NBD1 Domain with Atp

Enzymatic activity of Crystal Structure of Human DELTAF508 Human NBD1 Domain with Atp

All present enzymatic activity of Crystal Structure of Human DELTAF508 Human NBD1 Domain with Atp:
3.6.3.49;

Protein crystallography data

The structure of Crystal Structure of Human DELTAF508 Human NBD1 Domain with Atp, PDB code: 1xmj was solved by H.A.Lewis, X.Zhao, C.Wang, J.M.Sauder, I.Rooney, B.W.Noland, D.Lorimer, M.C.Kearins, K.Conners, B.Condon, P.C.Maloney, W.B.Guggino, J.F.Hunt, S.Emtage, Structural Genomix, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.74 / 2.30
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 59.793, 59.793, 144.398, 90.00, 90.00, 90.00
R / Rfree (%) 22 / 28.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human DELTAF508 Human NBD1 Domain with Atp (pdb code 1xmj). 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 Crystal Structure of Human DELTAF508 Human NBD1 Domain with Atp, PDB code: 1xmj:

Magnesium binding site 1 out of 1 in 1xmj

Go back to Magnesium Binding Sites List in 1xmj
Magnesium binding site 1 out of 1 in the Crystal Structure of Human DELTAF508 Human NBD1 Domain with Atp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Human DELTAF508 Human NBD1 Domain with Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2

b:43.2
occ:1.00
O2B A:ATP1 2.1 25.1 1.0
OG1 A:THR465 2.2 27.4 1.0
O2G A:ATP1 2.3 38.9 1.0
O A:HOH105 2.5 67.0 1.0
OE1 A:GLN493 2.8 38.4 1.0
PG A:ATP1 3.1 34.2 1.0
PB A:ATP1 3.2 26.1 1.0
CB A:THR465 3.3 25.2 1.0
O3B A:ATP1 3.3 34.3 1.0
O1G A:ATP1 3.4 44.2 1.0
O1A A:ATP1 3.7 33.6 1.0
CD A:GLN493 4.0 37.9 1.0
N A:THR465 4.0 23.6 1.0
OD2 A:ASP572 4.2 25.0 1.0
CA A:THR465 4.2 24.8 1.0
O3A A:ATP1 4.2 34.5 1.0
O1B A:ATP1 4.3 26.0 1.0
OD1 A:ASP572 4.3 28.6 1.0
CG2 A:THR465 4.3 23.2 1.0
O A:HOH33 4.4 27.4 1.0
PA A:ATP1 4.5 22.7 1.0
NE2 A:GLN493 4.5 35.7 1.0
O3G A:ATP1 4.6 46.2 1.0
CG A:ASP572 4.7 25.9 1.0
CE A:LYS464 5.0 22.0 1.0
CB A:LYS464 5.0 21.4 1.0

Reference:

H.A.Lewis, X.Zhao, C.Wang, J.M.Sauder, I.Rooney, B.W.Noland, D.Lorimer, M.C.Kearins, K.Conners, B.Condon, P.C.Maloney, W.B.Guggino, J.F.Hunt, S.Emtage. Impact of the Delta-F508 Mutation in First Nucleotide-Binding Domain of Human Cystic Fibrosis Transmembrane Conductance Regulator on Domain Folding and Structure J.Biol.Chem. V. 280 1346 2005.
ISSN: ISSN 0021-9258
PubMed: 15528182
DOI: 10.1074/JBC.M410968200
Page generated: Tue Aug 13 17:44:28 2024

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