Calcium in PDB 4a09: Structure of HSDDB1-DRDDB2 Bound to A 15 Bp Cpd-Duplex (Purine at D-1 Position) at 3.1 A Resolution (Cpd 2)

Protein crystallography data

The structure of Structure of HSDDB1-DRDDB2 Bound to A 15 Bp Cpd-Duplex (Purine at D-1 Position) at 3.1 A Resolution (Cpd 2), PDB code: 4a09 was solved by A.Scrima, E.S.Fischer, S.Iwai, H.Gut, N.H.Thoma, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.27 / 3.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 111.650, 122.940, 154.200, 90.00, 90.00, 90.00
R / Rfree (%) 24.5 / 30.8

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of HSDDB1-DRDDB2 Bound to A 15 Bp Cpd-Duplex (Purine at D-1 Position) at 3.1 A Resolution (Cpd 2) (pdb code 4a09). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Structure of HSDDB1-DRDDB2 Bound to A 15 Bp Cpd-Duplex (Purine at D-1 Position) at 3.1 A Resolution (Cpd 2), PDB code: 4a09:

Calcium binding site 1 out of 1 in 4a09

Go back to Calcium Binding Sites List in 4a09
Calcium binding site 1 out of 1 in the Structure of HSDDB1-DRDDB2 Bound to A 15 Bp Cpd-Duplex (Purine at D-1 Position) at 3.1 A Resolution (Cpd 2)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of HSDDB1-DRDDB2 Bound to A 15 Bp Cpd-Duplex (Purine at D-1 Position) at 3.1 A Resolution (Cpd 2) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca1456

b:31.9
occ:1.00
OH B:TYR331 3.0 38.7 1.0
CE1 B:HIS283 3.8 50.5 1.0
CE1 B:TYR331 3.9 38.6 1.0
CZ B:TYR331 3.9 38.5 1.0
NZ B:LYS433 3.9 32.8 1.0
ND1 B:HIS283 4.0 50.5 1.0
CD B:LYS378 4.6 35.0 1.0
CE B:LYS378 4.7 35.2 1.0
NE2 B:HIS283 4.9 50.5 1.0

Reference:

A.Scrima, E.S.Fischer, S.Iwai, H.Gut, N.H.Thoma. The Molecular Basis of CRL4(DDB2/Csa) Ubiquitin Ligase Architecture, Targeting, and Activation Cell(Cambridge,Mass.) V. 147 1024 2011.
ISSN: ISSN 0092-8674
PubMed: 22118460
DOI: 10.1016/J.CELL.2011.10.035
Page generated: Sat Dec 12 04:37:58 2020

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