Chlorine in PDB 3r4t: Crystal Structure of 4-Aminobutyrate Aminotransferase Gabt From Mycobacterium Marinum Covalently Bound to Pyridoxal Phosphate

The structure of Crystal Structure of 4-Aminobutyrate Aminotransferase Gabt From Mycobacterium Marinum Covalently Bound to Pyridoxal Phosphate, PDB code: 3r4t was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.50
Space group	P 62 2 2
Cell size a, b, c (Å), α, β, γ (°)	123.620, 123.620, 157.590, 90.00, 90.00, 120.00
R / Rfree (%)	15.1 / 19.1

The structure of Crystal Structure of 4-Aminobutyrate Aminotransferase Gabt From Mycobacterium Marinum Covalently Bound to Pyridoxal Phosphate also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of 4-Aminobutyrate Aminotransferase Gabt From Mycobacterium Marinum Covalently Bound to Pyridoxal Phosphate (pdb code 3r4t). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of 4-Aminobutyrate Aminotransferase Gabt From Mycobacterium Marinum Covalently Bound to Pyridoxal Phosphate, PDB code: 3r4t:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Crystal Structure of 4-Aminobutyrate Aminotransferase Gabt From Mycobacterium Marinum Covalently Bound to Pyridoxal Phosphate


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 4-Aminobutyrate Aminotransferase Gabt From Mycobacterium Marinum Covalently Bound to Pyridoxal Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl447 b:51.0 occ:1.00 NE A:ARG156 3.4 22.2 1.0 NH2 A:ARG156 3.4 19.5 1.0 O A:HOH557 3.5 12.9 1.0 O A:HOH554 3.5 21.4 1.0 OH A:TYR153 3.6 24.4 1.0 CZ A:ARG156 3.9 21.2 1.0 CZ A:TYR153 4.2 22.5 1.0 CE1 A:TYR170 4.3 25.0 1.0 CD A:ARG156 4.5 20.5 1.0 CE2 A:TYR153 4.6 20.9 1.0 CE1 A:TYR153 4.9 19.8 1.0 CD1 A:ILE65 5.0 21.4 1.0

Chlorine binding site 2 out of 4 in the Crystal Structure of 4-Aminobutyrate Aminotransferase Gabt From Mycobacterium Marinum Covalently Bound to Pyridoxal Phosphate


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 4-Aminobutyrate Aminotransferase Gabt From Mycobacterium Marinum Covalently Bound to Pyridoxal Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl448 b:59.4 occ:1.00 N A:LEU10 3.5 36.9 1.0 CA A:LEU9 4.0 36.0 1.0 C A:LEU9 4.3 36.0 1.0 O A:ARG8 4.3 36.7 1.0 CB A:LEU10 4.3 37.0 1.0 CD1 A:LEU9 4.3 35.2 1.0 CA A:LEU10 4.4 36.7 1.0 O A:LEU10 4.5 38.4 1.0 CG A:LEU10 4.6 37.7 1.0 N A:LEU9 4.7 35.4 1.0 C A:ARG8 4.8 36.0 1.0 C A:LEU10 4.9 37.8 1.0 CB A:LEU9 4.9 36.6 1.0

Chlorine binding site 3 out of 4 in the Crystal Structure of 4-Aminobutyrate Aminotransferase Gabt From Mycobacterium Marinum Covalently Bound to Pyridoxal Phosphate


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 4-Aminobutyrate Aminotransferase Gabt From Mycobacterium Marinum Covalently Bound to Pyridoxal Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl449 b:68.3 occ:1.00 CB A:PRO189 4.7 27.9 1.0 CG A:ASN193 4.8 37.9 1.0 O A:PRO189 4.8 28.3 1.0 C A:PRO189 4.8 28.1 1.0 ND2 A:ASN193 4.9 36.3 1.0 CB A:ASN193 4.9 35.6 1.0 O A:HOH539 5.0 23.4 1.0

Chlorine binding site 4 out of 4 in the Crystal Structure of 4-Aminobutyrate Aminotransferase Gabt From Mycobacterium Marinum Covalently Bound to Pyridoxal Phosphate


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 4-Aminobutyrate Aminotransferase Gabt From Mycobacterium Marinum Covalently Bound to Pyridoxal Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl450 b:73.6 occ:1.00 NH1 A:ARG352 3.5 34.2 1.0 CG A:ARG352 4.0 35.4 1.0 CD A:ARG352 4.1 38.2 1.0 NH1 A:ARG348 4.4 47.1 1.0 CZ A:ARG352 4.6 36.5 1.0 OE2 A:GLU351 4.8 40.0 1.0 NE A:ARG352 4.8 36.5 1.0 CD A:GLU351 4.8 37.1 1.0 CZ A:ARG348 4.9 46.7 1.0 O A:ARG348 4.9 31.8 1.0

L.Baugh, I.Phan, D.W.Begley, M.C.Clifton, B.Armour, D.M.Dranow, B.M.Taylor, M.M.Muruthi, J.Abendroth, J.W.Fairman, D.Fox, S.H.Dieterich, B.L.Staker, A.S.Gardberg, R.Choi, S.N.Hewitt, A.J.Napuli, J.Myers, L.K.Barrett, Y.Zhang, M.Ferrell, E.Mundt, K.Thompkins, N.Tran, S.Lyons-Abbott, A.Abramov, A.Sekar, D.Serbzhinskiy, D.Lorimer, G.W.Buchko, R.Stacy, L.J.Stewart, T.E.Edwards, W.C.Van Voorhis, P.J.Myler. Increasing the Structural Coverage of Tuberculosis Drug Targets. Tuberculosis (Edinb) V. 95 142 2015.
ISSN: ISSN 1472-9792
PubMed: 25613812
DOI: 10.1016/J.TUBE.2014.12.003