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Chlorine in PDB 6o12: E. Coli Cysteine Desulfurase Sufs H123A

Enzymatic activity of E. Coli Cysteine Desulfurase Sufs H123A

All present enzymatic activity of E. Coli Cysteine Desulfurase Sufs H123A:
2.8.1.7; 4.4.1.16;

Protein crystallography data

The structure of E. Coli Cysteine Desulfurase Sufs H123A, PDB code: 6o12 was solved by J.A.Dunkle, P.A.Frantom, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.40 / 2.05
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 127.280, 127.280, 134.163, 90.00, 90.00, 90.00
R / Rfree (%) 19.5 / 21.6

Chlorine Binding Sites:

The binding sites of Chlorine atom in the E. Coli Cysteine Desulfurase Sufs H123A (pdb code 6o12). 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 E. Coli Cysteine Desulfurase Sufs H123A, PDB code: 6o12:

Chlorine binding site 1 out of 1 in 6o12

Go back to Chlorine Binding Sites List in 6o12
Chlorine binding site 1 out of 1 in the E. Coli Cysteine Desulfurase Sufs H123A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of E. Coli Cysteine Desulfurase Sufs H123A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl502

b:37.3
occ:0.92
ND1 A:HIS124 3.2 34.1 1.0
CE1 A:HIS362 3.6 39.4 1.0
SG A:CYS364 3.6 51.3 1.0
CE1 A:HIS124 3.7 36.2 1.0
CA A:CYS364 4.1 37.1 1.0
CB A:CYS364 4.1 35.5 1.0
NE2 A:HIS362 4.3 46.2 1.0
CG A:HIS124 4.4 34.8 1.0
ND1 A:HIS362 4.6 39.9 1.0
N A:CYS364 4.8 33.8 1.0
CB A:HIS124 4.9 31.0 1.0
NE2 A:HIS124 5.0 34.1 1.0

Reference:

M.Blahut, C.E.Wise, M.R.Bruno, G.Dong, T.M.Makris, P.A.Frantom, J.A.Dunkle, F.W.Outten. Direct Observation of Intermediates in the Sufs Cysteine Desulfurase Reaction Reveals Functional Roles of Conserved Active-Site Residues. J.Biol.Chem. V. 294 12444 2019.
ISSN: ESSN 1083-351X
PubMed: 31248989
DOI: 10.1074/JBC.RA119.009471
Page generated: Mon Jul 29 12:27:08 2024

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