Calcium in PDB 3fvq: Crystal Structure of the Nucleotide Binding Domain Fbpc Complexed with Atp

All present enzymatic activity of Crystal Structure of the Nucleotide Binding Domain Fbpc Complexed with Atp:
3.6.3.30;

The structure of Crystal Structure of the Nucleotide Binding Domain Fbpc Complexed with Atp, PDB code: 3fvq was solved by S.Newstead, P.Bilton, E.P.Carpenter, D.Campopiano, S.Iwata, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	52.27 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.861, 89.095, 149.014, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 25.6

The binding sites of Calcium atom in the Crystal Structure of the Nucleotide Binding Domain Fbpc Complexed with Atp (pdb code 3fvq). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Crystal Structure of the Nucleotide Binding Domain Fbpc Complexed with Atp, PDB code: 3fvq:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Crystal Structure of the Nucleotide Binding Domain Fbpc Complexed with Atp


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of the Nucleotide Binding Domain Fbpc Complexed with Atp within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca360 b:9.1 occ:1.00 O1G A:ATP401 2.3 8.0 1.0 O A:HOH367 2.3 7.9 1.0 OG1 A:THR44 2.3 9.1 1.0 O2B A:ATP401 2.3 8.2 1.0 OE1 A:GLN87 2.4 10.8 1.0 O A:HOH385 2.5 8.3 1.0 CD A:GLN87 3.4 12.8 1.0 CB A:THR44 3.4 9.5 1.0 PB A:ATP401 3.5 9.2 1.0 PG A:ATP401 3.5 9.4 1.0 O3B A:ATP401 3.8 7.3 1.0 NE2 A:GLN87 3.9 11.7 1.0 OD2 A:ASP163 4.2 10.6 1.0 O B:HOH416 4.2 13.1 1.0 O1A A:ATP401 4.2 11.1 1.0 OD1 A:ASP163 4.3 11.6 1.0 O3G A:ATP401 4.3 6.7 1.0 N A:THR44 4.3 9.2 1.0 N B:GLY141 4.3 9.4 1.0 O A:HOH452 4.4 11.9 1.0 CA A:THR44 4.4 10.2 1.0 O A:HOH400 4.5 11.0 1.0 CG2 A:THR44 4.5 11.2 1.0 O3A A:ATP401 4.5 11.1 1.0 CG A:ASP163 4.6 10.3 1.0 CG A:GLN87 4.6 10.6 1.0 O1B A:ATP401 4.7 5.8 1.0 O2G A:ATP401 4.7 7.5 1.0 CB A:GLN87 4.7 12.3 1.0 PA A:ATP401 4.8 10.8 1.0 CA B:GLY141 4.8 8.9 1.0

Calcium binding site 2 out of 3 in the Crystal Structure of the Nucleotide Binding Domain Fbpc Complexed with Atp


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of the Nucleotide Binding Domain Fbpc Complexed with Atp within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca361 b:46.4 occ:1.00 O A:HOH509 3.5 36.1 1.0 O A:HOH577 3.8 26.0 1.0 O A:CYS257 4.6 25.7 1.0 C A:CYS257 4.7 26.2 1.0 CA A:ARG258 4.7 27.8 1.0 N A:ARG258 4.9 26.4 1.0 CG A:ARG258 5.0 30.3 1.0

Calcium binding site 3 out of 3 in the Crystal Structure of the Nucleotide Binding Domain Fbpc Complexed with Atp


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Crystal Structure of the Nucleotide Binding Domain Fbpc Complexed with Atp within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca361 b:5.7 occ:1.00 O1G B:ATP360 2.3 10.5 1.0 OG1 B:THR44 2.3 4.8 1.0 O2B B:ATP360 2.3 2.5 1.0 O B:HOH372 2.4 3.7 1.0 OE1 B:GLN87 2.4 7.5 1.0 O B:HOH408 2.4 3.6 1.0 CB B:THR44 3.4 4.5 1.0 CD B:GLN87 3.4 7.2 1.0 PG B:ATP360 3.5 6.9 1.0 PB B:ATP360 3.5 5.4 1.0 O3B B:ATP360 3.7 5.1 1.0 NE2 B:GLN87 3.9 8.6 1.0 O1A B:ATP360 4.1 3.6 1.0 OD2 B:ASP163 4.1 5.7 1.0 O3G B:ATP360 4.2 7.6 1.0 N B:THR44 4.2 6.1 1.0 OD1 B:ASP163 4.3 6.6 1.0 O B:HOH505 4.3 13.0 1.0 O B:HOH475 4.3 11.4 1.0 CA B:THR44 4.4 5.0 1.0 N A:GLY141 4.4 4.6 1.0 O B:HOH377 4.4 9.3 1.0 CG2 B:THR44 4.4 6.7 1.0 O3A B:ATP360 4.5 5.1 1.0 O1B B:ATP360 4.6 6.2 1.0 CG B:ASP163 4.6 6.1 1.0 CG B:GLN87 4.6 7.9 1.0 CB B:GLN87 4.7 9.0 1.0 O2G B:ATP360 4.7 7.3 1.0 PA B:ATP360 4.8 6.0 1.0 CA A:GLY141 5.0 4.8 1.0

S.Newstead, P.W.Fowler, P.Bilton, E.P.Carpenter, P.J.Sadler, D.J.Campopiano, M.S.Sansom, S.Iwata. Insights Into How Nucleotide-Binding Domains Power Abc Transport. Structure V. 17 1213 2009.
ISSN: ISSN 0969-2126
PubMed: 19748342
DOI: 10.1016/J.STR.2009.07.009