Atomistry » Zinc » PDB 6bmm-6bwy » 6bms
Atomistry »
  Zinc »
    PDB 6bmm-6bwy »
      6bms »

Zinc in PDB 6bms: Palmitoyltransferase Structure

Enzymatic activity of Palmitoyltransferase Structure

All present enzymatic activity of Palmitoyltransferase Structure:
2.3.1.225;

Protein crystallography data

The structure of Palmitoyltransferase Structure, PDB code: 6bms was solved by P.Kumar, K.Rajashankar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.21 / 2.44
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 186.402, 186.402, 90.177, 90.00, 90.00, 90.00
R / Rfree (%) 23.3 / 26.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Palmitoyltransferase Structure (pdb code 6bms). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Palmitoyltransferase Structure, PDB code: 6bms:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 6bms

Go back to Zinc Binding Sites List in 6bms
Zinc binding site 1 out of 4 in the Palmitoyltransferase Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Palmitoyltransferase Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:58.7
occ:1.00
ND1 A:HIS128 2.2 83.5 1.0
SG A:CYS115 2.4 55.3 1.0
SG A:CYS135 2.4 54.6 1.0
SG A:CYS118 2.5 63.5 1.0
CE1 A:HIS128 2.8 71.8 1.0
CG A:HIS128 3.0 71.9 1.0
N A:CYS135 3.2 55.7 1.0
CB A:CYS118 3.2 63.0 1.0
CB A:CYS135 3.4 49.8 1.0
CB A:CYS115 3.4 58.0 1.0
CB A:HIS128 3.5 50.0 1.0
CA A:CYS135 3.6 49.0 1.0
NE2 A:HIS128 3.7 77.0 1.0
CD2 A:HIS128 3.8 81.2 1.0
C A:THR134 3.9 55.1 1.0
N A:CYS118 4.0 66.9 1.0
CA A:HIS128 4.2 54.4 1.0
CA A:CYS118 4.3 64.5 1.0
CA A:THR134 4.4 67.6 1.0
O A:THR134 4.5 56.5 1.0
CA A:CYS115 4.9 63.4 1.0
CB A:ARG117 4.9 70.8 1.0

Zinc binding site 2 out of 4 in 6bms

Go back to Zinc Binding Sites List in 6bms
Zinc binding site 2 out of 4 in the Palmitoyltransferase Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Palmitoyltransferase Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1002

b:62.0
occ:1.00
SG A:CYS149 2.1 58.6 1.0
ND1 A:HIS142 2.2 70.5 1.0
SG A:CYS129 2.3 50.9 1.0
SG A:CYS132 2.3 72.2 1.0
CE1 A:HIS142 3.1 63.3 1.0
CG A:HIS142 3.1 70.7 1.0
CB A:CYS149 3.2 53.4 1.0
CB A:CYS129 3.3 48.3 1.0
CB A:CYS132 3.4 72.7 1.0
CB A:HIS142 3.4 45.9 1.0
N A:CYS132 3.7 64.3 1.0
CA A:CYS149 3.7 52.7 1.0
N A:CYS149 3.8 57.2 1.0
NE2 A:HIS142 4.1 73.0 1.0
CD2 A:HIS142 4.1 60.6 1.0
CA A:CYS132 4.1 58.0 1.0
CA A:HIS142 4.2 53.7 1.0
CB A:VAL131 4.4 66.4 1.0
C A:ASN148 4.5 64.2 1.0
CA A:CYS129 4.7 57.9 1.0
C A:VAL131 4.7 73.6 1.0
O A:ASN148 4.9 68.8 1.0
CA A:VAL131 5.0 65.3 1.0

Zinc binding site 3 out of 4 in 6bms

Go back to Zinc Binding Sites List in 6bms
Zinc binding site 3 out of 4 in the Palmitoyltransferase Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Palmitoyltransferase Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn1001

b:63.3
occ:1.00
ND1 D:HIS132 2.1 66.3 1.0
SG D:CYS119 2.4 63.4 1.0
SG D:CYS122 2.4 63.0 1.0
SG D:CYS139 2.5 57.1 1.0
CE1 D:HIS132 3.1 52.6 1.0
CG D:HIS132 3.1 65.2 1.0
CB D:CYS122 3.2 60.0 1.0
N D:CYS139 3.3 59.0 1.0
CB D:CYS139 3.4 50.0 1.0
CB D:CYS119 3.4 62.8 1.0
CB D:HIS132 3.5 54.9 1.0
CA D:CYS139 3.6 56.5 1.0
C D:THR138 3.9 68.4 1.0
N D:CYS122 4.0 63.9 1.0
NE2 D:HIS132 4.2 61.5 1.0
CA D:HIS132 4.2 60.1 1.0
CD2 D:HIS132 4.2 53.5 1.0
CA D:CYS122 4.3 58.2 1.0
CA D:THR138 4.5 71.6 1.0
O D:THR138 4.5 63.2 1.0
CA D:CYS119 4.8 54.3 1.0
N D:HIS132 5.0 55.1 1.0

Zinc binding site 4 out of 4 in 6bms

Go back to Zinc Binding Sites List in 6bms
Zinc binding site 4 out of 4 in the Palmitoyltransferase Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Palmitoyltransferase Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn1002

b:63.6
occ:1.00
CD2 D:HIS146 2.2 68.5 1.0
SG D:CYS133 2.3 58.4 1.0
SG D:CYS136 2.4 63.6 1.0
SG D:CYS153 2.4 60.0 1.0
CB D:CYS153 3.0 54.5 1.0
CG D:HIS146 3.2 62.7 1.0
NE2 D:HIS146 3.3 61.8 1.0
CB D:CYS133 3.3 58.3 1.0
CB D:CYS136 3.4 59.3 1.0
CA D:CYS153 3.5 59.1 1.0
CB D:HIS146 3.6 50.9 1.0
N D:CYS153 3.7 59.1 1.0
N D:CYS136 3.8 72.7 1.0
CA D:HIS146 4.1 51.8 1.0
CA D:CYS136 4.2 58.5 1.0
ND1 D:HIS146 4.3 63.8 1.0
CE1 D:HIS146 4.4 61.4 1.0
C D:ASN152 4.5 70.2 1.0
CB D:VAL135 4.7 63.3 1.0
CA D:CYS133 4.7 55.6 1.0
N D:HIS146 4.9 53.7 1.0
CE D:MET143 4.9 59.8 1.0
C D:VAL135 4.9 71.9 1.0
O D:ASN152 5.0 70.4 1.0
C D:CYS153 5.0 53.5 1.0

Reference:

M.S.Rana, P.Kumar, C.J.Lee, R.Verardi, K.R.Rajashankar, A.Banerjee. Fatty Acyl Recognition and Transfer By An Integral Membranes-Acyltransferase. Science V. 359 2018.
ISSN: ESSN 1095-9203
PubMed: 29326245
DOI: 10.1126/SCIENCE.AAO6326
Page generated: Wed Dec 16 11:32:40 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy