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Magnesium in PDB 2vqd: Crystal Structure of Biotin Carboxylase From Pseudomonas Aeruginosa Complexed with Ampcp

Enzymatic activity of Crystal Structure of Biotin Carboxylase From Pseudomonas Aeruginosa Complexed with Ampcp

All present enzymatic activity of Crystal Structure of Biotin Carboxylase From Pseudomonas Aeruginosa Complexed with Ampcp:
6.3.4.14;

Protein crystallography data

The structure of Crystal Structure of Biotin Carboxylase From Pseudomonas Aeruginosa Complexed with Ampcp, PDB code: 2vqd was solved by I.Mochalkin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 63.37 / 2.41
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 64.227, 126.786, 49.878, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 25.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Biotin Carboxylase From Pseudomonas Aeruginosa Complexed with Ampcp (pdb code 2vqd). 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 Biotin Carboxylase From Pseudomonas Aeruginosa Complexed with Ampcp, PDB code: 2vqd:

Magnesium binding site 1 out of 1 in 2vqd

Go back to Magnesium Binding Sites List in 2vqd
Magnesium binding site 1 out of 1 in the Crystal Structure of Biotin Carboxylase From Pseudomonas Aeruginosa Complexed with Ampcp


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 Biotin Carboxylase From Pseudomonas Aeruginosa Complexed with Ampcp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1449

b:39.8
occ:1.00
 OE2 A:GLU288 1.9 39.6 1.0
O A:HOH2139 2.0 35.7 1.0
O1B A:AP21448 2.0 36.9 1.0
O A:HOH2133 2.2 38.5 1.0
OE1 A:GLU276 2.4 36.9 1.0
O2A A:AP21448 2.4 35.9 1.0
CD A:GLU288 3.1 35.9 1.0
O A:HOH2231 3.1 41.9 1.0
CD A:GLU276 3.2 36.1 1.0
PB A:AP21448 3.2 35.4 1.0
OE2 A:GLU276 3.4 37.1 1.0
O3B A:AP21448 3.6 37.3 1.0
PA A:AP21448 3.7 34.5 1.0
O A:HOH2232 3.7 41.1 1.0
CG A:GLU288 3.8 35.7 1.0
O A:HOH2125 4.0 29.5 1.0
OE1 A:GLU288 4.0 36.3 1.0
C3A A:AP21448 4.1 35.4 1.0
C5' A:AP21448 4.2 33.9 1.0
OD1 A:ASN290 4.3 32.6 1.0
O A:HOH2122 4.3 31.9 1.0
O5' A:AP21448 4.4 33.5 1.0
O2B A:AP21448 4.5 37.3 1.0
CG A:GLU276 4.7 35.5 1.0
ND2 A:ASN290 4.7 32.3 1.0
CE1 A:HIS209 4.8 30.8 1.0
O1A A:AP21448 4.9 34.5 1.0
CG A:ASN290 5.0 32.7 1.0

Reference:

I.Mochalkin, J.R.Miller, A.Evdokimov, S.Lightle, C.Yan, C.K.Stover, G.L.Waldrop. Structural Evidence For Substrate-Induced Synergism and Half-Sites Reactivity in Biotin Carboxylase. Protein Sci. V. 17 1706 2008.
ISSN: ISSN 0961-8368
PubMed: 18725455
DOI: 10.1110/PS.035584.108
Page generated: Wed Aug 14 05:18:27 2024

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