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Calcium in PDB 5fq4: Crystal Structure of the Lipoprotein BT2263 From Bacteroides Thetaiotaomicron

Protein crystallography data

The structure of Crystal Structure of the Lipoprotein BT2263 From Bacteroides Thetaiotaomicron, PDB code: 5fq4 was solved by A.J.Glenwright, K.R.Pothula, D.S.Chorev, A.Basle, C.V.Robinson, U.Kleinekathoefer, D.N.Bolam, B.Van Den Berg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.54 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.757, 80.025, 120.047, 90.00, 100.12, 90.00
R / Rfree (%) 15.8 / 19.9

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Lipoprotein BT2263 From Bacteroides Thetaiotaomicron (pdb code 5fq4). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of the Lipoprotein BT2263 From Bacteroides Thetaiotaomicron, PDB code: 5fq4:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 5fq4

Go back to Calcium Binding Sites List in 5fq4
Calcium binding site 1 out of 2 in the Crystal Structure of the Lipoprotein BT2263 From Bacteroides Thetaiotaomicron


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 Lipoprotein BT2263 From Bacteroides Thetaiotaomicron within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca501

b:20.9
occ:1.00
O A:ARG408 2.3 19.4 1.0
OD2 A:ASP411 2.3 27.0 1.0
O A:LYS480 2.4 24.4 1.0
OD1 A:ASP478 2.4 19.7 1.0
O A:HOH2374 2.4 17.0 1.0
OD1 A:ASP411 2.5 20.8 1.0
O A:HOH2373 2.5 19.9 1.0
CG A:ASP411 2.7 23.4 1.0
CG A:ASP478 3.4 21.1 1.0
C A:ARG408 3.4 22.2 1.0
C A:LYS480 3.5 33.4 1.0
OD2 A:ASP478 3.9 21.4 1.0
O A:HOH2432 4.1 30.4 1.0
CG A:LYS480 4.1 46.8 1.0
OXT A:LYS480 4.1 36.2 1.0
O A:ARG409 4.1 18.3 1.0
CA A:ARG408 4.1 19.1 1.0
CB A:ASP411 4.2 21.1 1.0
N A:LYS480 4.3 28.0 1.0
CA A:LYS480 4.5 29.8 1.0
C A:ARG409 4.5 21.8 1.0
N A:ARG409 4.5 19.0 1.0
CB A:ASP478 4.6 19.9 1.0
CA A:ARG409 4.6 20.6 1.0
N A:ASP411 4.7 16.8 1.0
O A:ILE407 4.7 18.6 1.0
O A:HOH2176 4.8 21.9 1.0
CA A:ASP411 4.8 19.9 1.0
CA A:ASP478 4.8 18.1 1.0
O A:HOH2379 4.8 24.4 1.0
O A:HOH2380 4.9 40.2 1.0
CB A:ARG408 4.9 15.2 1.0
CB A:LYS480 4.9 36.2 1.0
O A:HOH2220 5.0 22.8 1.0

Calcium binding site 2 out of 2 in 5fq4

Go back to Calcium Binding Sites List in 5fq4
Calcium binding site 2 out of 2 in the Crystal Structure of the Lipoprotein BT2263 From Bacteroides Thetaiotaomicron


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 Lipoprotein BT2263 From Bacteroides Thetaiotaomicron within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca501

b:21.5
occ:1.00
O B:ARG408 2.3 18.9 1.0
OD1 B:ASP478 2.3 17.5 1.0
O B:LYS480 2.4 27.8 1.0
OD1 B:ASP411 2.5 25.2 1.0
O B:HOH2353 2.5 17.9 1.0
OD2 B:ASP411 2.5 26.4 1.0
O B:HOH2352 2.5 20.9 1.0
CG B:ASP411 2.8 24.0 1.0
CG B:ASP478 3.3 19.6 1.0
C B:ARG408 3.5 17.5 1.0
C B:LYS480 3.5 37.5 1.0
OD2 B:ASP478 3.8 21.9 1.0
CG B:LYS480 4.1 37.7 1.0
OXT B:LYS480 4.1 41.0 1.0
CA B:ARG408 4.1 17.1 1.0
O B:HOH2393 4.2 34.5 1.0
O B:ARG409 4.2 17.4 1.0
CB B:ASP411 4.3 22.3 1.0
N B:LYS480 4.3 29.6 1.0
CA B:LYS480 4.5 32.0 1.0
CB B:ASP478 4.5 23.2 1.0
N B:ARG409 4.5 15.4 1.0
C B:ARG409 4.5 21.4 1.0
CA B:ARG409 4.7 18.7 1.0
N B:ASP411 4.7 21.1 1.0
O B:HOH2355 4.7 22.0 1.0
O B:ILE407 4.8 21.6 1.0
CA B:ASP478 4.8 21.4 1.0
O B:HOH2179 4.8 21.6 1.0
CB B:ARG408 4.9 14.4 1.0
CA B:ASP411 4.9 20.9 1.0
CB B:LYS480 5.0 28.4 1.0
O B:HOH2208 5.0 17.7 1.0
CE B:LYS480 5.0 33.5 1.0
C B:ASP478 5.0 18.8 1.0
NZ B:LYS480 5.0 49.4 1.0

Reference:

A.J.Glenwright, K.R.Pothula, S.P.Bhamidimarri, D.S.Chorev, A.Basle, S.J.Firbank, H.Zheng, C.V.Robinson, M.Winterhalter, U.Kleinekathofer, D.N.Bolam, B.Van Den Berg. Structural Basis For Nutrient Acquisition By Dominant Members of the Human Gut Microbiota. Nature V. 541 407 2017.
ISSN: ESSN 1476-4687
PubMed: 28077872
DOI: 10.1038/NATURE20828
Page generated: Sun Jul 14 19:17:58 2024

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