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Chlorine in PDB 2r0c: Structure of the Substrate-Free Form of the Rebeccamycin Biosynthetic Enzyme Rebc

Protein crystallography data

The structure of Structure of the Substrate-Free Form of the Rebeccamycin Biosynthetic Enzyme Rebc, PDB code: 2r0c was solved by K.S.Ryan, C.L.Drennan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 63.220, 77.562, 64.673, 90.00, 108.04, 90.00
R / Rfree (%) 21.1 / 24.1

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of the Substrate-Free Form of the Rebeccamycin Biosynthetic Enzyme Rebc (pdb code 2r0c). 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 Structure of the Substrate-Free Form of the Rebeccamycin Biosynthetic Enzyme Rebc, PDB code: 2r0c:

Chlorine binding site 1 out of 1 in 2r0c

Go back to Chlorine Binding Sites List in 2r0c
Chlorine binding site 1 out of 1 in the Structure of the Substrate-Free Form of the Rebeccamycin Biosynthetic Enzyme Rebc


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of the Substrate-Free Form of the Rebeccamycin Biosynthetic Enzyme Rebc within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1429

b:57.1
occ:1.00
O A:HOH1407 3.1 69.0 1.0
OH A:TYR167 3.2 32.5 1.0
NH1 A:ARG290 3.6 34.8 1.0
O A:HOH1349 3.6 41.4 1.0
CE2 A:TYR167 3.9 31.4 1.0
CZ A:TYR167 3.9 32.6 1.0
NH2 A:ARG290 3.9 35.2 1.0
CZ A:ARG290 4.2 36.1 1.0
CD A:ARG166 4.3 47.9 1.0
CD2 A:LEU327 4.3 32.1 1.0
CG2 A:THR326 4.6 32.5 1.0
O A:THR326 4.7 32.1 1.0
O A:HOH1288 4.7 52.8 1.0
O A:HOH1199 4.8 42.7 1.0
CB A:ARG166 4.8 37.4 1.0
CA A:LEU327 4.8 35.3 1.0

Reference:

K.S.Ryan, A.R.Howard-Jones, M.J.Hamill, S.J.Elliott, C.T.Walsh, C.L.Drennan. Crystallographic Trapping in the Rebeccamycin Biosynthetic Enzyme Rebc Proc.Natl.Acad.Sci.Usa V. 104 15311 2007.
ISSN: ISSN 0027-8424
PubMed: 17873060
DOI: 10.1073/PNAS.0707190104
Page generated: Sat Dec 12 09:17:58 2020

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