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Chlorine in PDB 6q8e: Crystal Structure of Branched-Chain Amino Acid Aminotransferase From Thermobaculum Terrenum in Pmp-Form

Enzymatic activity of Crystal Structure of Branched-Chain Amino Acid Aminotransferase From Thermobaculum Terrenum in Pmp-Form

All present enzymatic activity of Crystal Structure of Branched-Chain Amino Acid Aminotransferase From Thermobaculum Terrenum in Pmp-Form:
2.6.1.42;

Protein crystallography data

The structure of Crystal Structure of Branched-Chain Amino Acid Aminotransferase From Thermobaculum Terrenum in Pmp-Form, PDB code: 6q8e was solved by K.M.Boyko, E.Y.Bezsudnova, A.Y.Nikolaeva, Y.S.Zeifman, T.V.Rakitina, V.O.Popov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.83 / 1.50
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 144.750, 144.750, 144.500, 90.00, 90.00, 120.00
R / Rfree (%) 14 / 17.6

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Branched-Chain Amino Acid Aminotransferase From Thermobaculum Terrenum in Pmp-Form (pdb code 6q8e). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 5 binding sites of Chlorine where determined in the Crystal Structure of Branched-Chain Amino Acid Aminotransferase From Thermobaculum Terrenum in Pmp-Form, PDB code: 6q8e:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5;

Chlorine binding site 1 out of 5 in 6q8e

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Chlorine binding site 1 out of 5 in the Crystal Structure of Branched-Chain Amino Acid Aminotransferase From Thermobaculum Terrenum in Pmp-Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Branched-Chain Amino Acid Aminotransferase From Thermobaculum Terrenum in Pmp-Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl402

b:26.3
occ:1.00
 OH A:TYR101 3.1 22.5 1.0
O A:HOH731 3.2 34.2 1.0
N A:HIS261 3.3 18.4 1.0
C4A A:PMP401 3.5 20.4 1.0
O A:HOH676 3.5 22.6 1.0
N4A A:PMP401 3.6 21.7 1.0
CB A:HIS261 3.7 22.6 1.0
O A:HOH777 3.7 49.2 1.0
CB A:THR260 3.7 17.9 1.0
CE1 A:TYR101 3.9 21.2 1.0
O A:HOH604 3.9 19.1 1.0
CZ A:TYR101 3.9 19.9 1.0
O2P A:PMP401 4.0 16.5 1.0
N A:THR260 4.0 17.5 1.0
CA A:HIS261 4.1 20.3 1.0
CA A:THR260 4.1 17.4 1.0
C A:THR260 4.2 17.6 1.0
CA A:GLY41 4.3 17.2 1.0
O A:HOH648 4.5 27.5 1.0
OG1 A:THR260 4.6 18.0 1.0
CG2 A:THR260 4.6 19.8 1.0
C A:GLY41 4.8 18.3 1.0
O A:GLY41 4.8 17.3 1.0
N A:GLY41 4.9 16.6 1.0
NZ A:LYS161 4.9 22.8 1.0
CG A:HIS261 5.0 25.9 1.0
C A:GLY259 5.0 18.8 1.0

Chlorine binding site 2 out of 5 in 6q8e

Go back to Chlorine Binding Sites List in 6q8e
Chlorine binding site 2 out of 5 in the Crystal Structure of Branched-Chain Amino Acid Aminotransferase From Thermobaculum Terrenum in Pmp-Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Branched-Chain Amino Acid Aminotransferase From Thermobaculum Terrenum in Pmp-Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl403

b:46.5
occ:1.00
 O A:HOH718 2.9 32.0 1.0
O A:HOH653 3.0 34.2 1.0
O A:HOH811 3.2 47.5 1.0
CA A:PRO8 3.7 21.9 1.0
CD A:PRO130 3.9 21.9 1.0
CB A:TYR96 3.9 25.8 1.0
CG A:PRO130 4.0 23.0 1.0
CB A:PRO8 4.0 24.2 1.0
CG A:TYR96 4.2 23.9 1.0
N A:PRO8 4.4 23.6 1.0
CG A:PRO8 4.4 24.7 1.0
CD1 A:TYR96 4.4 29.4 1.0
O A:ASN7 4.8 26.0 1.0
N A:LYS9 4.9 22.6 1.0
C A:PRO8 4.9 21.1 1.0
C A:ASN7 4.9 26.1 1.0
CD2 A:TYR96 4.9 24.3 1.0
CB A:ASN94 4.9 19.4 1.0
N A:PRO130 5.0 20.8 1.0

Chlorine binding site 3 out of 5 in 6q8e

Go back to Chlorine Binding Sites List in 6q8e
Chlorine binding site 3 out of 5 in the Crystal Structure of Branched-Chain Amino Acid Aminotransferase From Thermobaculum Terrenum in Pmp-Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Branched-Chain Amino Acid Aminotransferase From Thermobaculum Terrenum in Pmp-Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl404

b:33.3
occ:1.00
 O A:HOH723 3.0 40.2 1.0
O A:HOH864 3.0 38.4 1.0
O A:HOH672 3.0 35.4 1.0
O A:HOH717 3.1 24.0 1.0
O A:ARG272 3.5 22.3 1.0
CA A:ARG272 3.7 19.3 1.0
C A:ARG272 3.7 19.4 1.0
CB A:SER269 3.7 17.5 1.0
OG A:SER269 4.0 18.4 1.0
N A:GLU274 4.1 18.8 1.0
CB A:GLU274 4.2 22.5 1.0
CB A:ARG272 4.2 17.0 1.0
O A:HOH780 4.3 36.6 1.0
N A:HIS273 4.3 18.7 1.0
CA A:GLU274 4.5 18.9 1.0
CD A:ARG272 4.5 19.5 1.0
C A:HIS273 4.5 18.2 1.0
O A:HOH511 4.6 25.1 1.0
OE2 A:GLU274 4.6 43.8 1.0
O A:HOH834 4.6 44.9 1.0
CA A:HIS273 4.8 18.0 1.0
O A:HOH857 4.8 53.8 1.0
O A:HOH703 4.9 36.3 1.0
N A:ARG272 4.9 16.4 1.0

Chlorine binding site 4 out of 5 in 6q8e

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Chlorine binding site 4 out of 5 in the Crystal Structure of Branched-Chain Amino Acid Aminotransferase From Thermobaculum Terrenum in Pmp-Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of Branched-Chain Amino Acid Aminotransferase From Thermobaculum Terrenum in Pmp-Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl405

b:37.2
occ:1.00
 O A:HOH568 2.8 40.6 1.0
NH1 A:ARG232 3.2 27.1 1.0
O A:HOH726 3.6 50.1 1.0
CE1 A:HIS229 3.7 32.8 1.0
ND1 A:HIS229 3.7 33.5 1.0
CD A:ARG232 3.7 28.0 1.0
NE2 A:HIS229 3.9 31.7 1.0
CG A:HIS229 3.9 25.8 1.0
CG2 A:ILE228 4.0 20.7 1.0
CD2 A:HIS229 4.1 27.3 1.0
CZ A:ARG232 4.2 24.1 1.0
CA A:HIS229 4.2 22.0 1.0
O A:HOH542 4.3 46.6 1.0
NE A:ARG232 4.4 25.7 1.0
N A:HIS229 4.4 21.0 1.0
OE2 A:GLU233 4.6 32.1 1.0
C A:ILE228 4.6 21.1 1.0
O A:ILE228 4.6 22.1 1.0
CB A:HIS229 4.7 23.1 1.0
CG A:ARG232 4.8 24.7 1.0
CB A:ARG232 4.9 25.1 1.0

Chlorine binding site 5 out of 5 in 6q8e

Go back to Chlorine Binding Sites List in 6q8e
Chlorine binding site 5 out of 5 in the Crystal Structure of Branched-Chain Amino Acid Aminotransferase From Thermobaculum Terrenum in Pmp-Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Crystal Structure of Branched-Chain Amino Acid Aminotransferase From Thermobaculum Terrenum in Pmp-Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl406

b:34.6
occ:1.00
 N A:VAL239 3.2 24.0 1.0
NE A:ARG232 3.2 25.7 1.0
O A:VAL239 3.5 26.3 1.0
NH2 A:ARG232 3.7 26.9 1.0
CA A:GLU238 3.7 24.9 1.0
CZ A:ARG232 3.8 24.1 1.0
C A:GLU238 3.9 24.2 1.0
CD A:ARG232 4.1 28.0 1.0
CA A:VAL239 4.2 21.7 1.0
O A:LEU237 4.2 28.6 1.0
CG A:ARG232 4.2 24.7 1.0
C A:VAL239 4.3 21.2 1.0
CB A:GLU238 4.3 29.1 1.0
O A:HOH573 4.3 53.4 1.0
CG A:GLU238 4.4 32.2 0.5
CB A:VAL239 4.4 24.4 1.0
N A:GLU238 4.7 24.7 1.0
CG2 A:VAL239 4.8 26.2 1.0
C A:LEU237 4.9 24.4 1.0
CG A:GLU238 4.9 32.1 0.5

Reference:

E.Y.Bezsudnova, K.M.Boyko, A.Y.Nikolaeva, Y.S.Zeifman, T.V.Rakitina, D.A.Suplatov, V.O.Popov. Biochemical and Structural Insights Into Plp Fold Type IV Transaminase From Thermobaculum Terrenum. Biochimie V. 158 130 2018.
ISSN: ISSN 1638-6183
PubMed: 30599183
DOI: 10.1016/J.BIOCHI.2018.12.017
Page generated: Sat Jul 12 18:47:44 2025

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