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Calcium in PDB 1hqd: Pseudomonas Cepacia Lipase Complexed with Transition State Analogue of 1-Phenoxy-2-Acetoxy Butane

Enzymatic activity of Pseudomonas Cepacia Lipase Complexed with Transition State Analogue of 1-Phenoxy-2-Acetoxy Butane

All present enzymatic activity of Pseudomonas Cepacia Lipase Complexed with Transition State Analogue of 1-Phenoxy-2-Acetoxy Butane:
3.1.1.3;

Protein crystallography data

The structure of Pseudomonas Cepacia Lipase Complexed with Transition State Analogue of 1-Phenoxy-2-Acetoxy Butane, PDB code: 1hqd was solved by M.Luic, S.Tomic, I.Lescic, E.Ljubovic, D.Sepac, V.Sunjic, L.Vitale, W.Saenger, B.Kojic-Prodic, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.30
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 89.060, 46.630, 84.300, 90.00, 120.86, 90.00
R / Rfree (%) 15.4 / 20.3

Calcium Binding Sites:

The binding sites of Calcium atom in the Pseudomonas Cepacia Lipase Complexed with Transition State Analogue of 1-Phenoxy-2-Acetoxy Butane (pdb code 1hqd). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Pseudomonas Cepacia Lipase Complexed with Transition State Analogue of 1-Phenoxy-2-Acetoxy Butane, PDB code: 1hqd:

Calcium binding site 1 out of 1 in 1hqd

Go back to Calcium Binding Sites List in 1hqd
Calcium binding site 1 out of 1 in the Pseudomonas Cepacia Lipase Complexed with Transition State Analogue of 1-Phenoxy-2-Acetoxy Butane


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Pseudomonas Cepacia Lipase Complexed with Transition State Analogue of 1-Phenoxy-2-Acetoxy Butane within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca613

b:15.4
occ:1.00
 O A:GLN292 2.3 16.3 1.0
OD2 A:ASP242 2.3 12.5 1.0
OD1 A:ASP288 2.3 11.8 1.0
O A:HOH409 2.3 8.2 1.0
O A:VAL296 2.4 13.5 1.0
O A:HOH326 2.6 6.2 1.0
C A:GLN292 3.3 15.8 1.0
CG A:ASP242 3.4 12.4 1.0
CG A:ASP288 3.5 11.2 1.0
N A:LEU293 3.5 15.4 1.0
C A:VAL296 3.6 12.5 1.0
CA A:ARG297 4.2 12.2 1.0
OG A:SER244 4.2 11.4 1.0
OD1 A:ASP242 4.2 13.0 1.0
CB A:ASP242 4.3 12.0 1.0
OD2 A:ASP288 4.3 11.5 1.0
CA A:ASP288 4.3 10.0 1.0
ND2 A:ASN285 4.3 10.5 1.0
N A:ASP288 4.3 9.3 1.0
OD1 A:ASN285 4.3 12.1 1.0
N A:ARG297 4.3 12.2 1.0
O A:HOH374 4.4 10.1 1.0
OG1 A:THR245 4.5 12.1 1.0
CB A:ASP288 4.5 11.1 1.0
CA A:VAL296 4.7 12.9 1.0
CA A:GLN292 4.7 15.8 1.0
C A:LEU287 4.7 10.0 1.0
CB A:ARG297 4.7 12.6 1.0
CG A:ASN285 4.8 10.8 1.0
CB A:LEU287 4.9 10.7 1.0
CB A:VAL296 4.9 12.8 1.0
N A:VAL296 4.9 13.3 1.0
N A:GLN292 5.0 15.3 1.0
CA A:LEU293 5.0 15.7 1.0

Reference:

M.Luic, S.Tomic, I.Lescic, E.Ljubovic, D.Sepac, V.Sunjic, L.Vitale, W.Saenger, B.Kojic-Prodic. Complex of Burkholderia Cepacia Lipase with Transition State Analogue of 1-Phenoxy-2-Acetoxybutane: Biocatalytic, Structural and Modelling Study. Eur.J.Biochem. V. 268 3964 2001.
ISSN: ISSN 0014-2956
PubMed: 11453990
DOI: 10.1046/J.1432-1327.2001.02303.X
Page generated: Mon Jul 7 15:40:49 2025

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