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Calcium in PDB 6wbx: Single-Particle Cryo-Em Structure of Arabinofuranosyltransferase Aftd From Mycobacteria, Mutant R1389S Class 1

Calcium Binding Sites:

The binding sites of Calcium atom in the Single-Particle Cryo-Em Structure of Arabinofuranosyltransferase Aftd From Mycobacteria, Mutant R1389S Class 1 (pdb code 6wbx). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Single-Particle Cryo-Em Structure of Arabinofuranosyltransferase Aftd From Mycobacteria, Mutant R1389S Class 1, PDB code: 6wbx:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 6wbx

Go back to Calcium Binding Sites List in 6wbx
Calcium binding site 1 out of 2 in the Single-Particle Cryo-Em Structure of Arabinofuranosyltransferase Aftd From Mycobacteria, Mutant R1389S Class 1


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Single-Particle Cryo-Em Structure of Arabinofuranosyltransferase Aftd From Mycobacteria, Mutant R1389S Class 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca2001

b:38.2
occ:1.00
O A:THR743 2.4 36.1 1.0
OG1 A:THR743 2.4 36.1 1.0
O A:ASP740 2.5 38.9 1.0
O A:ALA735 2.5 31.7 1.0
OE2 A:GLU839 2.6 37.6 1.0
O A:THR838 2.6 35.5 1.0
OD1 A:ASP738 2.7 36.7 1.0
O A:ASP738 3.1 36.7 1.0
C A:THR743 3.5 36.1 1.0
C A:ASP740 3.6 38.9 1.0
CD A:GLU839 3.6 37.6 1.0
C A:ALA735 3.7 31.7 1.0
CB A:THR743 3.7 36.1 1.0
CG A:ASP738 3.8 36.7 1.0
C A:THR838 3.8 35.5 1.0
C A:ASP738 4.0 36.7 1.0
N A:ASP740 4.1 38.9 1.0
CA A:THR743 4.1 36.1 1.0
OE1 A:GLU839 4.3 37.6 1.0
CA A:ASP740 4.3 38.9 1.0
N A:THR743 4.3 36.1 1.0
CA A:ALA736 4.4 32.5 1.0
OD2 A:ASP738 4.4 36.7 1.0
N A:ALA736 4.5 32.5 1.0
CA A:THR838 4.5 35.5 1.0
CG A:GLU839 4.5 37.6 1.0
CB A:ASP740 4.6 38.9 1.0
N A:ILE737 4.6 36.1 1.0
N A:SER744 4.6 33.0 1.0
N A:ASP738 4.6 36.7 1.0
C A:ALA736 4.6 32.5 1.0
N A:ASN741 4.7 37.9 1.0
CA A:ASP738 4.7 36.7 1.0
C A:ARG739 4.7 42.1 1.0
CA A:ALA735 4.7 31.7 1.0
CB A:THR838 4.7 35.5 1.0
CB A:ASP738 4.8 36.7 1.0
CG2 A:THR743 4.8 36.1 1.0
N A:GLU839 4.8 37.6 1.0
CA A:ASN741 4.9 37.9 1.0
N A:ARG739 4.9 42.1 1.0
CA A:SER744 5.0 33.0 1.0

Calcium binding site 2 out of 2 in 6wbx

Go back to Calcium Binding Sites List in 6wbx
Calcium binding site 2 out of 2 in the Single-Particle Cryo-Em Structure of Arabinofuranosyltransferase Aftd From Mycobacteria, Mutant R1389S Class 1


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Single-Particle Cryo-Em Structure of Arabinofuranosyltransferase Aftd From Mycobacteria, Mutant R1389S Class 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca2002

b:51.5
occ:1.00
O A:ALA962 2.2 51.5 1.0
O A:THR970 2.2 48.3 1.0
O A:ASP967 2.3 51.8 1.0
OD1 A:ASP965 2.3 55.2 1.0
OG1 A:THR970 2.4 48.3 1.0
O A:ALA1075 2.5 52.7 1.0
CG A:ASP965 3.3 55.2 1.0
C A:THR970 3.3 48.3 1.0
C A:ALA962 3.3 51.5 1.0
C A:ASP967 3.5 51.8 1.0
OD2 A:ASP965 3.5 55.2 1.0
CB A:THR970 3.6 48.3 1.0
C A:ALA1075 3.7 52.7 1.0
CA A:THR970 3.8 48.3 1.0
N A:THR970 3.9 48.3 1.0
CA A:ALA962 4.0 51.5 1.0
CB A:ALA962 4.1 51.5 1.0
N A:ASP967 4.1 51.8 1.0
CA A:ASP967 4.2 51.8 1.0
CB A:ASP967 4.3 51.8 1.0
N A:ASP965 4.4 55.2 1.0
N A:ALA963 4.4 54.7 1.0
N A:VAL971 4.5 49.0 1.0
N A:PRO968 4.5 50.0 1.0
CA A:ALA1075 4.5 52.7 1.0
CG2 A:THR970 4.5 48.3 1.0
CB A:ASP965 4.6 55.2 1.0
CA A:ALA963 4.6 54.7 1.0
C A:ALA963 4.7 54.7 1.0
CA A:PRO968 4.7 50.0 1.0
N A:GLU1076 4.7 57.7 1.0
CA A:GLU1076 4.8 57.7 1.0
CB A:GLU1076 4.8 57.7 1.0
N A:THR964 4.9 58.8 1.0
N A:GLY969 4.9 47.3 1.0
CA A:ASP965 4.9 55.2 1.0
CA A:VAL971 4.9 49.0 1.0
C A:PRO968 4.9 50.0 1.0
O A:ALA963 5.0 54.7 1.0

Reference:

Y.Z.Tan, L.Zhang, J.Rodrigues, R.B.Zheng, S.I.Giacometti, A.L.Rosario, B.Kloss, V.P.Dandey, H.Wei, R.Brunton, A.M.Raczkowski, D.Athayde, M.J.Catalao, M.Pimentel, O.B.Clarke, T.L.Lowary, M.Archer, M.Niederweis, C.S.Potter, B.Carragher, F.Mancia. Cryo-Em Structures and Regulation of Arabinofuranosyltransferase Aftd From Mycobacteria Mol.Cell 2020.
ISSN: ISSN 1097-2765
DOI: 10.1016/J.MOLCEL.2020.04.014
Page generated: Tue Jul 16 17:23:14 2024

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