Atomistry » Cobalt » PDB 4xim-5d6e » 5b7y
Atomistry »
  Cobalt »
    PDB 4xim-5d6e »
      5b7y »

Cobalt in PDB 5b7y: Crystal Structure of Hyperthermophilic Thermotoga Maritima L-Ketose-3- Epimerase with CO2+

Protein crystallography data

The structure of Crystal Structure of Hyperthermophilic Thermotoga Maritima L-Ketose-3- Epimerase with CO2+, PDB code: 5b7y was solved by T.P.Cao, S.M.Shin, D.W.Lee, S.H.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.15 / 1.32
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 50.284, 55.255, 58.754, 107.14, 102.35, 92.20
R / Rfree (%) 17.1 / 18.9

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Crystal Structure of Hyperthermophilic Thermotoga Maritima L-Ketose-3- Epimerase with CO2+ (pdb code 5b7y). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Crystal Structure of Hyperthermophilic Thermotoga Maritima L-Ketose-3- Epimerase with CO2+, PDB code: 5b7y:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 5b7y

Go back to Cobalt Binding Sites List in 5b7y
Cobalt binding site 1 out of 2 in the Crystal Structure of Hyperthermophilic Thermotoga Maritima L-Ketose-3- Epimerase with CO2+


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of Hyperthermophilic Thermotoga Maritima L-Ketose-3- Epimerase with CO2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co303

b:10.5
occ:1.00
OE2 A:GLU149 2.0 10.3 1.0
OD2 A:ASP182 2.0 9.7 1.0
ND1 A:HIS208 2.1 9.8 1.0
OE2 A:GLU243 2.1 11.2 1.0
O A:HOH438 2.1 15.7 1.0
CD A:GLU149 2.9 11.1 1.0
CE1 A:HIS208 3.0 11.0 1.0
CD A:GLU243 3.1 13.5 1.0
CG A:ASP182 3.1 9.8 1.0
CG A:HIS208 3.1 9.4 1.0
OE1 A:GLU149 3.2 11.8 1.0
OE1 A:GLU243 3.4 14.4 1.0
CB A:HIS208 3.5 9.5 1.0
CB A:ASP182 3.5 10.2 1.0
O A:HOH529 3.9 15.6 1.0
NH2 A:ARG214 4.0 12.4 1.0
NE2 A:HIS208 4.2 10.0 1.0
OD1 A:ASP182 4.2 11.4 1.0
CD2 A:HIS208 4.2 10.4 1.0
O A:HOH534 4.2 11.6 1.0
CD2 A:HIS185 4.3 10.9 1.0
CG A:GLU149 4.3 9.8 1.0
CG A:GLU243 4.4 12.9 1.0
NE2 A:HIS185 4.5 10.9 1.0
CD2 A:LEU180 4.7 16.4 1.0
CB A:GLU243 4.7 11.7 1.0
CA A:ASP182 4.8 9.6 1.0
CA A:HIS208 5.0 9.8 1.0

Cobalt binding site 2 out of 2 in 5b7y

Go back to Cobalt Binding Sites List in 5b7y
Cobalt binding site 2 out of 2 in the Crystal Structure of Hyperthermophilic Thermotoga Maritima L-Ketose-3- Epimerase with CO2+


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Crystal Structure of Hyperthermophilic Thermotoga Maritima L-Ketose-3- Epimerase with CO2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Co302

b:11.1
occ:1.00
OE2 B:GLU149 2.0 11.6 1.0
OD2 B:ASP182 2.1 11.1 1.0
OE2 B:GLU243 2.1 13.0 1.0
ND1 B:HIS208 2.1 10.9 1.0
O B:HOH417 2.1 15.6 1.0
CD B:GLU149 2.9 11.0 1.0
CD B:GLU243 3.0 14.0 1.0
CE1 B:HIS208 3.0 10.9 1.0
CG B:ASP182 3.1 11.0 1.0
CG B:HIS208 3.1 10.1 1.0
OE1 B:GLU149 3.2 12.7 1.0
OE1 B:GLU243 3.3 14.6 1.0
CB B:HIS208 3.4 11.0 1.0
CB B:ASP182 3.5 10.7 1.0
O B:HOH528 3.8 16.4 1.0
NH2 B:ARG214 4.0 13.7 1.0
NE2 B:HIS208 4.2 12.1 1.0
OD1 B:ASP182 4.2 12.0 1.0
O B:HOH554 4.2 13.0 1.0
CD2 B:HIS208 4.2 11.2 1.0
CG B:GLU149 4.3 10.1 1.0
CD2 B:HIS185 4.3 11.2 1.0
CG B:GLU243 4.4 13.8 1.0
NE2 B:HIS185 4.5 12.1 1.0
CB B:GLU243 4.7 11.5 1.0
CA B:ASP182 4.8 10.5 1.0
CA B:HIS208 5.0 11.4 1.0

Reference:

S.M.Shin, T.P.Cao, J.M.Choi, S.B.Kim, S.J.Lee, S.H.Lee, D.W.Lee. TM0416, A Hyperthermophilic Promiscuous Nonphosphorylated Sugar Isomerase, Catalyzes Various C5AND C6EPIMERIZATION Reactions Appl. Environ. Microbiol. V. 83 2017.
ISSN: ESSN 1098-5336
PubMed: 28258150
DOI: 10.1128/AEM.03291-16
Page generated: Sun Dec 13 10:46:43 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy