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Cobalt in PDB 2fgp: Crystal Structure of A Minimal, All Rna Hairpin Ribozyme with Modifications (G8DAP, U39C) at pH 8.6

Protein crystallography data

The structure of Crystal Structure of A Minimal, All Rna Hairpin Ribozyme with Modifications (G8DAP, U39C) at pH 8.6, PDB code: 2fgp was solved by J.D.Salter, J.E.Wedekind, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.37 / 2.40
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.770, 93.770, 127.610, 90.00, 90.00, 120.00
R / Rfree (%) 24.8 / 25.9

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Crystal Structure of A Minimal, All Rna Hairpin Ribozyme with Modifications (G8DAP, U39C) at pH 8.6 (pdb code 2fgp). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Crystal Structure of A Minimal, All Rna Hairpin Ribozyme with Modifications (G8DAP, U39C) at pH 8.6, PDB code: 2fgp:

Cobalt binding site 1 out of 1 in 2fgp

Go back to Cobalt Binding Sites List in 2fgp
Cobalt binding site 1 out of 1 in the Crystal Structure of A Minimal, All Rna Hairpin Ribozyme with Modifications (G8DAP, U39C) at pH 8.6


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of A Minimal, All Rna Hairpin Ribozyme with Modifications (G8DAP, U39C) at pH 8.6 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Co11

b:55.5
occ:1.00
CO C:NCO11 0.0 55.5 1.0
N5 C:NCO11 2.0 59.1 1.0
N4 C:NCO11 2.0 59.1 1.0
N3 C:NCO11 2.0 59.5 1.0
N2 C:NCO11 2.0 55.7 1.0
N6 C:NCO11 2.0 61.3 1.0
N1 C:NCO11 2.0 55.3 1.0
OP1 D:A40 3.7 86.8 1.0
OP2 C:A20 3.8 0.1 1.0
OP2 D:U41 3.9 73.6 1.0
O6 C:G21 4.2 75.3 1.0
N7 C:G21 4.4 74.8 1.0
P D:A40 4.7 90.6 1.0
OP2 D:A40 4.9 88.4 1.0

Reference:

J.D.Salter, J.Krucinska, S.Alam, V.Grum-Tokars, J.E.Wedekind. Water in the Active Site of An All-Rna Hairpin Ribozyme and Effects of GUA8 Base Variants on the Geometry of Phosphoryl Transfer. Biochemistry V. 45 686 2006.
ISSN: ISSN 0006-2960
PubMed: 16411744
DOI: 10.1021/BI051887K
Page generated: Tue Jul 30 15:09:25 2024

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