Calcium in PDB 4uyp: High Resolution Structure of the Third Cohesin Scac in Complex with the Scab Dockerin with A Mutation in the N- Terminal Helix (in to Si) From Acetivibrio Cellulolyticus Displaying A Type I Interaction.

The structure of High Resolution Structure of the Third Cohesin Scac in Complex with the Scab Dockerin with A Mutation in the N- Terminal Helix (in to Si) From Acetivibrio Cellulolyticus Displaying A Type I Interaction., PDB code: 4uyp was solved by K.Cameron, V.D.Alves, P.Bule, L.M.A.Ferreira, C.M.G.A.Fontes, S.Najmudin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	76.19 / 1.49
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	107.750, 107.750, 100.810, 90.00, 90.00, 90.00
R / Rfree (%)	15.548 / 18.536

The binding sites of Calcium atom in the High Resolution Structure of the Third Cohesin Scac in Complex with the Scab Dockerin with A Mutation in the N- Terminal Helix (in to Si) From Acetivibrio Cellulolyticus Displaying A Type I Interaction. (pdb code 4uyp). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the High Resolution Structure of the Third Cohesin Scac in Complex with the Scab Dockerin with A Mutation in the N- Terminal Helix (in to Si) From Acetivibrio Cellulolyticus Displaying A Type I Interaction., PDB code: 4uyp:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in the High Resolution Structure of the Third Cohesin Scac in Complex with the Scab Dockerin with A Mutation in the N- Terminal Helix (in to Si) From Acetivibrio Cellulolyticus Displaying A Type I Interaction.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of High Resolution Structure of the Third Cohesin Scac in Complex with the Scab Dockerin with A Mutation in the N- Terminal Helix (in to Si) From Acetivibrio Cellulolyticus Displaying A Type I Interaction. within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca200 b:13.2 occ:1.00 OD1 B:ASP42 2.3 14.4 1.0 O B:SER48 2.3 15.5 1.0 OD1 B:ASP44 2.3 14.2 1.0 OD2 B:ASP53 2.4 11.7 1.0 O B:HOH2069 2.4 11.7 1.0 OD1 B:ASN46 2.4 15.3 1.0 OD1 B:ASP53 2.6 12.6 1.0 CG B:ASP53 2.9 11.7 1.0 CG B:ASP44 3.3 14.3 1.0 CG B:ASN46 3.3 14.7 1.0 CG B:ASP42 3.5 15.8 1.0 C B:SER48 3.6 13.3 1.0 OD2 B:ASP44 3.9 15.1 1.0 ND2 B:ASN46 3.9 18.7 1.0 N B:ASN46 4.2 19.7 1.0 CA B:ASP42 4.2 12.6 1.0 N B:SER48 4.3 14.9 1.0 OD2 B:ASP42 4.3 18.4 1.0 CB B:ASP42 4.3 14.2 1.0 CB B:ASP53 4.4 11.1 1.0 N B:ASP44 4.4 14.6 1.0 CB B:ASN46 4.4 20.2 1.0 CA B:ILE49 4.5 11.4 0.5 CA B:ILE49 4.5 12.1 0.5 N B:ILE49 4.5 12.3 1.0 CB B:ASP44 4.5 17.0 1.0 CA B:SER48 4.5 14.2 1.0 N B:LYS50 4.5 11.7 1.0 C B:ASP42 4.6 14.1 1.0 N B:GLY45 4.6 16.4 1.0 OD1 B:ASN52 4.7 11.7 1.0 CA B:ASP44 4.7 18.3 1.0 CA B:ASN46 4.7 20.9 1.0 N B:GLY47 4.8 18.2 1.0 N B:VAL43 4.8 12.5 1.0 C B:ASP44 4.9 17.9 1.0 C B:ILE49 4.9 12.3 1.0

Calcium binding site 2 out of 4 in the High Resolution Structure of the Third Cohesin Scac in Complex with the Scab Dockerin with A Mutation in the N- Terminal Helix (in to Si) From Acetivibrio Cellulolyticus Displaying A Type I Interaction.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of High Resolution Structure of the Third Cohesin Scac in Complex with the Scab Dockerin with A Mutation in the N- Terminal Helix (in to Si) From Acetivibrio Cellulolyticus Displaying A Type I Interaction. within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca201 b:14.7 occ:1.00 OD1 B:ASP8 2.3 16.1 1.0 OD1 B:ASP6 2.3 14.3 1.0 O B:SER12 2.4 16.0 1.0 OD2 B:ASP17 2.4 13.6 1.0 OD1 B:ASN10 2.4 16.4 1.0 O B:HOH2013 2.4 13.2 1.0 OD1 B:ASP17 2.6 14.3 1.0 CG B:ASP17 2.9 14.9 1.0 CG B:ASP8 3.3 15.5 1.0 CG B:ASN10 3.3 15.4 1.0 CG B:ASP6 3.5 15.0 1.0 C B:SER12 3.6 15.9 1.0 OD2 B:ASP8 3.7 16.6 1.0 ND2 B:ASN10 3.9 18.6 1.0 CA B:ASP6 4.1 13.8 1.0 N B:ASN10 4.2 17.0 1.0 N B:SER12 4.2 18.2 1.0 CB B:ASP6 4.3 14.7 1.0 C B:ASP6 4.3 15.9 1.0 OD2 B:ASP6 4.4 17.4 1.0 N B:ASP8 4.4 14.6 1.0 CB B:ASP17 4.4 13.2 1.0 CB B:ASN10 4.4 16.6 1.0 CG B:ARG14 4.4 17.7 1.0 CA B:SER12 4.5 17.2 0.5 N B:VAL13 4.5 15.4 1.0 CA B:VAL13 4.5 14.4 1.0 N B:ARG14 4.5 14.3 1.0 CA B:SER12 4.5 16.2 0.5 N B:VAL7 4.5 14.3 1.0 CB B:ASP8 4.5 16.3 1.0 N B:GLY9 4.6 16.8 1.0 CA B:ASN10 4.7 18.3 1.0 OG B:SER12 4.7 17.0 0.5 CB B:SER12 4.7 19.5 0.5 CA B:ASP8 4.7 15.1 1.0 CB B:ARG14 4.8 15.7 1.0 C B:ASP8 4.8 17.1 1.0 N B:GLY11 4.9 18.4 1.0 O B:ASP6 4.9 17.2 1.0 C B:VAL13 5.0 15.5 1.0 C B:ASN10 5.0 17.2 1.0

Calcium binding site 3 out of 4 in the High Resolution Structure of the Third Cohesin Scac in Complex with the Scab Dockerin with A Mutation in the N- Terminal Helix (in to Si) From Acetivibrio Cellulolyticus Displaying A Type I Interaction.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of High Resolution Structure of the Third Cohesin Scac in Complex with the Scab Dockerin with A Mutation in the N- Terminal Helix (in to Si) From Acetivibrio Cellulolyticus Displaying A Type I Interaction. within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca200 b:14.2 occ:1.00 OD1 D:ASP42 2.3 15.4 1.0 OD2 D:ASP53 2.3 12.4 1.0 OD1 D:ASP44 2.3 12.8 1.0 O D:SER48 2.4 16.8 1.0 O D:HOH2055 2.4 13.6 1.0 OD1 D:ASN46 2.4 16.0 1.0 OD1 D:ASP53 2.6 13.3 1.0 CG D:ASP53 2.9 14.7 1.0 CG D:ASP44 3.3 12.4 1.0 CG D:ASN46 3.3 16.4 1.0 CG D:ASP42 3.4 16.3 1.0 C D:SER48 3.6 16.3 1.0 OD2 D:ASP44 3.9 14.9 1.0 ND2 D:ASN46 4.0 26.4 1.0 N D:ASN46 4.2 19.0 1.0 N D:SER48 4.2 14.7 1.0 CA D:ASP42 4.2 15.1 1.0 OD2 D:ASP42 4.2 18.1 1.0 CB D:ASP42 4.3 16.2 1.0 CB D:ASN46 4.4 17.2 1.0 N D:ASP44 4.4 16.4 1.0 CB D:ASP53 4.4 12.5 1.0 CA D:ILE49 4.4 14.9 0.5 CB D:ASP44 4.5 17.6 1.0 N D:ILE49 4.5 14.9 1.0 CA D:SER48 4.5 15.9 0.5 CA D:SER48 4.5 15.1 0.5 N D:LYS50 4.5 12.4 1.0 C D:ASP42 4.5 16.0 1.0 CA D:ILE49 4.5 14.7 0.5 OD1 D:ASN52 4.6 11.4 1.0 N D:GLY45 4.6 18.3 1.0 CA D:ASN46 4.7 16.4 1.0 OG D:SER48 4.7 14.4 0.5 CA D:ASP44 4.7 17.5 1.0 N D:VAL43 4.8 14.1 1.0 N D:GLY47 4.8 16.9 1.0 C D:ASP44 4.8 17.1 1.0 O A:HOH2198 4.9 23.1 1.0 C D:ASN46 4.9 16.6 1.0 C D:ILE49 4.9 14.6 1.0 CB D:SER48 5.0 16.4 0.5

Calcium binding site 4 out of 4 in the High Resolution Structure of the Third Cohesin Scac in Complex with the Scab Dockerin with A Mutation in the N- Terminal Helix (in to Si) From Acetivibrio Cellulolyticus Displaying A Type I Interaction.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of High Resolution Structure of the Third Cohesin Scac in Complex with the Scab Dockerin with A Mutation in the N- Terminal Helix (in to Si) From Acetivibrio Cellulolyticus Displaying A Type I Interaction. within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca201 b:14.5 occ:1.00 OD1 D:ASP6 2.3 14.9 1.0 O D:SER12 2.3 16.7 1.0 O D:HOH2012 2.3 13.5 1.0 OD1 D:ASP8 2.4 15.0 1.0 OD1 D:ASN10 2.4 16.0 1.0 OD2 D:ASP17 2.5 13.9 1.0 OD1 D:ASP17 2.6 13.4 1.0 CG D:ASP17 2.9 12.7 1.0 CG D:ASN10 3.4 16.8 1.0 CG D:ASP8 3.4 17.0 1.0 CG D:ASP6 3.5 17.0 1.0 C D:SER12 3.5 15.5 1.0 OD2 D:ASP8 3.7 18.2 1.0 ND2 D:ASN10 4.0 16.9 1.0 CA D:ASP6 4.1 14.0 1.0 N D:ASN10 4.2 17.9 1.0 N D:SER12 4.2 18.0 1.0 CB D:ASP6 4.2 14.7 1.0 C D:ASP6 4.4 15.5 1.0 OD2 D:ASP6 4.4 19.3 1.0 N D:ASP8 4.4 14.4 1.0 CB D:ASP17 4.4 12.4 1.0 N D:VAL13 4.4 15.3 1.0 CB D:ASN10 4.4 18.4 1.0 CG D:ARG14 4.5 16.6 1.0 CA D:SER12 4.5 17.9 0.5 CA D:SER12 4.5 15.8 0.5 CA D:VAL13 4.5 13.8 1.0 N D:ARG14 4.5 13.8 1.0 N D:VAL7 4.6 14.3 1.0 N D:GLY9 4.6 17.2 1.0 OG D:SER12 4.6 14.3 0.5 CB D:ASP8 4.6 15.8 1.0 CA D:ASN10 4.7 18.2 1.0 CA D:ASP8 4.8 16.6 1.0 CB D:ARG14 4.8 14.6 1.0 N D:GLY11 4.9 17.7 1.0 O D:HOH2020 4.9 13.5 1.0 C D:ASP8 4.9 18.4 1.0 CB D:SER12 4.9 20.8 0.5 O D:ASP6 5.0 15.9 1.0 C D:VAL13 5.0 15.0 1.0 C D:ASN10 5.0 20.3 1.0

K.Cameron, S.Najmudin, V.D.Alves, E.A.Bayer, S.P.Smith, P.Bule, H.Waller, L.M.A.Ferreira, H.J.Gilbert, C.M.G.A.Fontes. Cell-Surface Attachment of Bacterial Multi-Enzyme Complexes Involves Highly Dynamic Protein-Protein Anchors. J.Biol.Chem. 2015.
ISSN: ESSN 1083-351X
PubMed: 25855788
DOI: 10.1074/JBC.M114.633339