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Calcium in PDB 1qge: New Crystal Form of Pseudomonas Glumae (Formerly Chromobacterium Viscosum Atcc 6918) Lipase

Enzymatic activity of New Crystal Form of Pseudomonas Glumae (Formerly Chromobacterium Viscosum Atcc 6918) Lipase

All present enzymatic activity of New Crystal Form of Pseudomonas Glumae (Formerly Chromobacterium Viscosum Atcc 6918) Lipase:
3.1.1.3;

Protein crystallography data

The structure of New Crystal Form of Pseudomonas Glumae (Formerly Chromobacterium Viscosum Atcc 6918) Lipase, PDB code: 1qge was solved by D.A.Lang, P.Stadler, A.Kovacs, F.Paltauf, B.W.Dijkstra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.980, 43.350, 140.690, 90.00, 90.00, 90.00
R / Rfree (%) 18.7 / 22.8

Calcium Binding Sites:

The binding sites of Calcium atom in the New Crystal Form of Pseudomonas Glumae (Formerly Chromobacterium Viscosum Atcc 6918) Lipase (pdb code 1qge). 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 New Crystal Form of Pseudomonas Glumae (Formerly Chromobacterium Viscosum Atcc 6918) Lipase, PDB code: 1qge:

Calcium binding site 1 out of 1 in 1qge

Go back to Calcium Binding Sites List in 1qge
Calcium binding site 1 out of 1 in the New Crystal Form of Pseudomonas Glumae (Formerly Chromobacterium Viscosum Atcc 6918) Lipase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of New Crystal Form of Pseudomonas Glumae (Formerly Chromobacterium Viscosum Atcc 6918) Lipase within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ca320

b:2.0
occ:1.00
 O E:HOH330 2.4 2.0 1.0
OD2 E:ASP241 2.4 4.6 1.0
O E:VAL295 2.5 6.0 1.0
O E:HOH321 2.5 2.0 1.0
OD1 E:ASP287 2.6 2.2 1.0
O E:GLN291 2.6 2.0 1.0
C E:VAL295 3.6 4.8 1.0
CG E:ASP241 3.6 3.7 1.0
C E:GLN291 3.7 2.8 1.0
CG E:ASP287 3.8 4.7 1.0
N E:LEU292 3.8 2.0 1.0
CA E:ARG296 4.0 3.9 1.0
OG E:SER243 4.2 3.6 1.0
N E:ARG296 4.3 3.8 1.0
OD1 E:ASP241 4.3 2.8 1.0
CB E:ASP241 4.3 4.0 1.0
O E:HOH323 4.4 3.6 1.0
OG1 E:THR244 4.4 2.0 1.0
OD1 E:ASN284 4.5 2.0 1.0
OD2 E:ASP287 4.5 2.2 1.0
ND2 E:ASN284 4.5 2.1 1.0
CA E:ASP287 4.6 3.0 1.0
N E:ASP287 4.6 2.7 1.0
CB E:ARG296 4.6 5.7 1.0
CA E:VAL295 4.6 5.0 1.0
CB E:VAL295 4.7 4.7 1.0
CB E:ASP287 4.8 2.9 1.0
CG1 E:VAL295 4.8 6.4 1.0
CA E:GLN291 4.9 2.0 1.0
CG E:ASN284 4.9 3.3 1.0
N E:VAL295 5.0 4.6 1.0
C E:LEU286 5.0 2.6 1.0

Reference:

D.A.Lang, P.Stadler, A.Kovacs, F.Paltauf, B.W.Dijkstra. Structural and Kinetic Investigations of Enantiomeric Binding Mode of Subclass I Lipases From the Family of Pseudomonadaceae To Be Published.
Page generated: Tue Jul 8 01:17:41 2025

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