Atomistry » Cobalt » PDB 1nyi-1rr2 » 1rl4
Atomistry »
  Cobalt »
    PDB 1nyi-1rr2 »
      1rl4 »

Cobalt in PDB 1rl4: Plasmodium Falciparum Peptide Deformylase Complex with Inhibitor

Enzymatic activity of Plasmodium Falciparum Peptide Deformylase Complex with Inhibitor

All present enzymatic activity of Plasmodium Falciparum Peptide Deformylase Complex with Inhibitor:
3.5.1.31;

Protein crystallography data

The structure of Plasmodium Falciparum Peptide Deformylase Complex with Inhibitor, PDB code: 1rl4 was solved by M.A.Robien, K.T.Nguyen, A.Kumar, I.Hirsh, S.Turley, D.Pei, W.G.J.Hol, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.18
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 102.317, 102.317, 118.339, 90.00, 90.00, 120.00
R / Rfree (%) 19.7 / 21.2

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Plasmodium Falciparum Peptide Deformylase Complex with Inhibitor (pdb code 1rl4). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Plasmodium Falciparum Peptide Deformylase Complex with Inhibitor, PDB code: 1rl4:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 1rl4

Go back to Cobalt Binding Sites List in 1rl4
Cobalt binding site 1 out of 2 in the Plasmodium Falciparum Peptide Deformylase Complex with Inhibitor


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Plasmodium Falciparum Peptide Deformylase Complex with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co301

b:27.9
occ:1.00
O4 A:BRR401 1.8 30.5 1.0
NE2 A:HIS202 2.0 22.4 1.0
NE2 A:HIS198 2.1 27.6 1.0
O1 A:BRR401 2.4 30.2 1.0
SG A:CYS156 2.4 24.7 1.0
N3 A:BRR401 2.8 30.1 1.0
C2 A:BRR401 3.0 26.0 1.0
CD2 A:HIS202 3.0 22.7 1.0
CD2 A:HIS198 3.0 22.1 1.0
CE1 A:HIS202 3.1 22.1 1.0
CE1 A:HIS198 3.2 27.9 1.0
NE2 A:GLN112 3.2 24.8 1.0
CB A:CYS156 3.5 19.9 1.0
O A:HOH707 3.8 24.3 1.0
CD A:GLN112 3.9 36.6 1.0
CA A:CYS156 3.9 26.3 1.0
OE1 A:GLN112 4.0 34.9 1.0
CG A:HIS202 4.1 27.5 1.0
C5 A:BRR401 4.1 29.7 1.0
ND1 A:HIS202 4.2 21.7 1.0
CG A:HIS198 4.2 26.1 1.0
ND1 A:HIS198 4.3 30.3 1.0
N A:LEU157 4.3 29.2 1.0
C6 A:BRR401 4.5 42.0 1.0
C A:CYS156 4.6 29.4 1.0
C7 A:BRR401 4.8 43.1 1.0
O A:HOH704 4.9 22.6 1.0
O A:GLY155 5.0 36.8 1.0

Cobalt binding site 2 out of 2 in 1rl4

Go back to Cobalt Binding Sites List in 1rl4
Cobalt binding site 2 out of 2 in the Plasmodium Falciparum Peptide Deformylase Complex with Inhibitor


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Plasmodium Falciparum Peptide Deformylase Complex with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Co1301

b:30.1
occ:1.00
O4 B:BRR1401 1.8 31.3 1.0
NE2 B:HIS202 2.0 24.9 1.0
NE2 B:HIS198 2.1 34.3 1.0
SG B:CYS156 2.3 26.4 1.0
O1 B:BRR1401 2.4 31.2 1.0
N3 B:BRR1401 2.8 31.8 1.0
CD2 B:HIS202 3.0 26.2 1.0
C2 B:BRR1401 3.0 29.2 1.0
CD2 B:HIS198 3.0 22.2 1.0
CE1 B:HIS202 3.1 28.0 1.0
CE1 B:HIS198 3.1 31.3 1.0
NE2 B:GLN112 3.3 26.7 1.0
CB B:CYS156 3.5 21.2 1.0
O B:HOH1707 3.8 25.3 1.0
CA B:CYS156 3.9 26.7 1.0
CD B:GLN112 3.9 38.4 1.0
OE1 B:GLN112 4.1 36.4 1.0
CG B:HIS202 4.1 27.7 1.0
C5 B:BRR1401 4.2 30.5 1.0
ND1 B:HIS202 4.2 23.6 1.0
CG B:HIS198 4.2 25.7 1.0
ND1 B:HIS198 4.2 29.7 1.0
N B:LEU157 4.3 31.4 1.0
C B:CYS156 4.5 30.2 1.0
C6 B:BRR1401 4.5 41.8 1.0
C7 B:BRR1401 4.7 40.0 1.0
O B:HOH1704 4.8 26.1 1.0
O B:GLY155 4.9 36.8 1.0
N B:SER158 5.0 30.7 1.0

Reference:

M.A.Robien, K.T.Nguyen, A.Kumar, I.Hirsh, S.Turley, D.Pei, W.G.J.Hol. An Improved Crystal Form of Plasmodium Falciparum Peptide Deformylase. Protein Sci. V. 13 1155 2004.
ISSN: ISSN 0961-8368
PubMed: 15010544
DOI: 10.1110/PS.03456404
Page generated: Tue Jul 30 14:34:50 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy