Atomistry » Chlorine » PDB 4egp-4emw » 4els
Atomistry »
  Chlorine »
    PDB 4egp-4emw »
      4els »

Chlorine in PDB 4els: Structure of E. Coli. 1,4-Dihydroxy-2- Naphthoyl Coenzyme A Synthases (Menb) in Complex with Bicarbonate

Enzymatic activity of Structure of E. Coli. 1,4-Dihydroxy-2- Naphthoyl Coenzyme A Synthases (Menb) in Complex with Bicarbonate

All present enzymatic activity of Structure of E. Coli. 1,4-Dihydroxy-2- Naphthoyl Coenzyme A Synthases (Menb) in Complex with Bicarbonate:
4.1.3.36;

Protein crystallography data

The structure of Structure of E. Coli. 1,4-Dihydroxy-2- Naphthoyl Coenzyme A Synthases (Menb) in Complex with Bicarbonate, PDB code: 4els was solved by Y.R.Sun, H.G.Song, J.Li, M.Jiang, Y.Li, J.H.Zhou, Z.H.Guo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.85 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 76.367, 133.888, 153.250, 90.00, 90.00, 90.00
R / Rfree (%) 18.2 / 22.2

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of E. Coli. 1,4-Dihydroxy-2- Naphthoyl Coenzyme A Synthases (Menb) in Complex with Bicarbonate (pdb code 4els). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 5 binding sites of Chlorine where determined in the Structure of E. Coli. 1,4-Dihydroxy-2- Naphthoyl Coenzyme A Synthases (Menb) in Complex with Bicarbonate, PDB code: 4els:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5;

Chlorine binding site 1 out of 5 in 4els

Go back to Chlorine Binding Sites List in 4els
Chlorine binding site 1 out of 5 in the Structure of E. Coli. 1,4-Dihydroxy-2- Naphthoyl Coenzyme A Synthases (Menb) in Complex with Bicarbonate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of E. Coli. 1,4-Dihydroxy-2- Naphthoyl Coenzyme A Synthases (Menb) in Complex with Bicarbonate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl304

b:44.5
occ:1.00
O C:HOH452 3.0 37.2 1.0
O A:HOH477 3.1 33.1 1.0
O D:HOH426 3.2 37.7 1.0
O1 A:EDO303 3.2 49.3 1.0
C1 A:EDO303 4.1 42.6 1.0
CA D:ARG173 4.3 30.3 1.0
CA A:ARG173 4.4 25.3 1.0
O A:ALA172 4.4 28.5 1.0
CD A:ARG173 4.4 27.2 1.0
CA C:ARG173 4.4 22.8 1.0
CD D:ARG173 4.4 24.9 1.0
CD C:ARG173 4.4 23.3 1.0
O C:ALA172 4.5 29.0 1.0
O D:ALA172 4.5 26.2 1.0
O D:ARG173 4.5 31.4 1.0
O A:ARG173 4.6 29.5 1.0
O C:ARG173 4.6 30.2 1.0
C D:ARG173 4.8 30.0 1.0
C A:ARG173 4.8 30.2 1.0
C C:ARG173 4.8 24.1 1.0

Chlorine binding site 2 out of 5 in 4els

Go back to Chlorine Binding Sites List in 4els
Chlorine binding site 2 out of 5 in the Structure of E. Coli. 1,4-Dihydroxy-2- Naphthoyl Coenzyme A Synthases (Menb) in Complex with Bicarbonate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of E. Coli. 1,4-Dihydroxy-2- Naphthoyl Coenzyme A Synthases (Menb) in Complex with Bicarbonate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl303

b:60.7
occ:1.00
CD B:PRO50 3.9 40.9 1.0
N B:LEU51 4.0 35.0 1.0
CD B:ARG49 4.1 27.6 1.0
CB B:PRO50 4.2 39.7 1.0
CG B:PRO50 4.3 50.3 1.0
N B:PRO50 4.3 36.4 1.0
CB B:LEU51 4.3 36.6 1.0
CG B:ARG49 4.3 38.9 1.0
CB B:ARG49 4.4 30.8 1.0
CA B:PRO50 4.7 42.9 1.0
CA B:LEU51 4.7 41.2 1.0
C B:PRO50 4.8 40.0 1.0
NE B:ARG49 4.8 37.0 1.0

Chlorine binding site 3 out of 5 in 4els

Go back to Chlorine Binding Sites List in 4els
Chlorine binding site 3 out of 5 in the Structure of E. Coli. 1,4-Dihydroxy-2- Naphthoyl Coenzyme A Synthases (Menb) in Complex with Bicarbonate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure of E. Coli. 1,4-Dihydroxy-2- Naphthoyl Coenzyme A Synthases (Menb) in Complex with Bicarbonate within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl303

b:60.9
occ:1.00
CD C:ARG49 3.9 34.2 1.0
CB C:LEU51 4.0 32.7 1.0
N C:LEU51 4.2 36.7 1.0
NH1 C:ARG49 4.4 42.2 1.0
NE C:ARG49 4.4 45.9 1.0
CG C:ARG49 4.5 40.6 1.0
CZ C:ARG49 4.6 48.6 1.0
CA C:LEU51 4.7 41.8 1.0
CD C:PRO50 4.7 49.9 1.0
CB C:ARG49 4.8 37.5 1.0
CB C:PRO50 4.9 45.2 1.0
CL C:CL304 5.0 81.6 1.0
N C:PRO50 5.0 48.6 1.0

Chlorine binding site 4 out of 5 in 4els

Go back to Chlorine Binding Sites List in 4els
Chlorine binding site 4 out of 5 in the Structure of E. Coli. 1,4-Dihydroxy-2- Naphthoyl Coenzyme A Synthases (Menb) in Complex with Bicarbonate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Structure of E. Coli. 1,4-Dihydroxy-2- Naphthoyl Coenzyme A Synthases (Menb) in Complex with Bicarbonate within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl304

b:81.6
occ:1.00
OE1 C:GLU23 3.8 62.6 1.0
OE2 C:GLU23 4.5 94.1 1.0
NH1 C:ARG49 4.5 42.2 1.0
CD2 C:LEU51 4.5 41.6 1.0
CD C:GLU23 4.5 78.8 1.0
NH2 C:ARG49 4.6 51.5 1.0
CZ C:ARG49 4.8 48.6 1.0
CL C:CL303 5.0 60.9 1.0

Chlorine binding site 5 out of 5 in 4els

Go back to Chlorine Binding Sites List in 4els
Chlorine binding site 5 out of 5 in the Structure of E. Coli. 1,4-Dihydroxy-2- Naphthoyl Coenzyme A Synthases (Menb) in Complex with Bicarbonate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Structure of E. Coli. 1,4-Dihydroxy-2- Naphthoyl Coenzyme A Synthases (Menb) in Complex with Bicarbonate within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl303

b:68.8
occ:1.00
NH2 D:ARG173 2.9 22.5 1.0
O C:HOH401 3.0 45.2 1.0
O D:HOH458 3.1 26.5 1.0
O D:ASP239 3.5 26.9 1.0
O D:CYS240 3.7 29.3 1.0
CZ D:ARG173 4.0 32.4 1.0
CA D:CYS240 4.1 22.4 1.0
C D:CYS240 4.1 29.2 1.0
NH1 D:ARG173 4.3 22.4 1.0
C D:ASP239 4.4 29.8 1.0
OD1 C:ASP239 4.6 29.6 1.0
N D:CYS240 4.6 20.0 1.0
C2 A:EDO305 4.6 56.9 1.0
O1 A:EDO305 4.7 37.6 1.0
O C:HOH409 4.9 31.7 1.0
O C:ASP239 5.0 20.3 1.0
C1 A:EDO305 5.0 56.7 1.0
NH2 A:ARG173 5.0 21.0 1.0

Reference:

Y.R.Sun, H.G.Song, J.Li, M.Jiang, Y.Li, J.H.Zhou, Z.H.Guo. Active Site Binding and Catalytic Role of Bicarbonate in 1,4-Dihydroxy-2-Naphthoyl Coenzyme A Synthases From Vitamin K Biosynthetic Pathways Biochemistry V. 51 4580 2012.
ISSN: ISSN 0006-2960
PubMed: 22606952
DOI: 10.1021/BI300486J
Page generated: Fri Jul 11 14:54:24 2025

Last articles

Mg in 4G5G
Mg in 4G3S
Mg in 4G3D
Mg in 4G3X
Mg in 4G3P
Mg in 4G3Q
Mg in 4G2L
Mg in 4G2Y
Mg in 4G2W
Mg in 4G2J
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy