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Chlorine in PDB 4pkc: Benzylsuccinate Alpha-Gamma Complex

Enzymatic activity of Benzylsuccinate Alpha-Gamma Complex

All present enzymatic activity of Benzylsuccinate Alpha-Gamma Complex:
4.1.99.11;

Protein crystallography data

The structure of Benzylsuccinate Alpha-Gamma Complex, PDB code: 4pkc was solved by M.A.Funk, C.L.Drennan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.97 / 2.60
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 154.864, 154.864, 82.171, 90.00, 90.00, 90.00
R / Rfree (%) 21.7 / 25.7

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Benzylsuccinate Alpha-Gamma Complex (pdb code 4pkc). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Benzylsuccinate Alpha-Gamma Complex, PDB code: 4pkc:

Chlorine binding site 1 out of 1 in 4pkc

Go back to Chlorine Binding Sites List in 4pkc
Chlorine binding site 1 out of 1 in the Benzylsuccinate Alpha-Gamma Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Benzylsuccinate Alpha-Gamma Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl901

b:86.0
occ:1.00
N A:SER495 2.9 75.2 1.0
N A:LEU492 3.2 72.5 1.0
N A:MET494 3.3 89.0 1.0
CB A:LEU492 3.3 77.8 1.0
CB A:SER495 3.4 79.1 1.0
N A:CYS493 3.4 74.6 1.0
CG A:MET494 3.5 0.7 1.0
CA A:LEU492 3.6 69.2 1.0
CA A:SER495 3.7 78.7 1.0
C A:LEU492 3.7 74.3 1.0
C A:MET494 3.9 75.2 1.0
CA A:MET494 4.0 84.6 1.0
O A:SER495 4.1 72.2 1.0
C A:CYS493 4.3 84.0 1.0
CG A:LEU492 4.3 65.4 1.0
CB A:MET494 4.3 88.7 1.0
CB A:VAL491 4.4 63.1 1.0
C A:VAL491 4.4 67.3 1.0
CA A:CYS493 4.4 84.5 1.0
C A:SER495 4.4 71.7 1.0
OG A:SER495 4.6 88.8 1.0
O A:LEU492 4.6 83.0 1.0
SD A:MET494 4.6 0.8 1.0
N A:VAL491 4.7 68.9 1.0
CA A:VAL491 4.7 62.7 1.0
CD1 A:LEU492 4.8 75.5 1.0
O A:HOH1183 5.0 77.1 1.0

Reference:

M.A.Funk, E.T.Judd, E.N.Marsh, S.J.Elliott, C.L.Drennan. Structures of Benzylsuccinate Synthase Elucidate Roles of Accessory Subunits in Glycyl Radical Enzyme Activation and Activity. Proc.Natl.Acad.Sci.Usa V. 111 10161 2014.
ISSN: ESSN 1091-6490
PubMed: 24982148
DOI: 10.1073/PNAS.1405983111
Page generated: Fri Jul 26 00:05:44 2024

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