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Calcium in PDB 6n5w: Crystal Structure of the CA2+/Cam Complex with Independent Peptides of KV7.4 (KCNQ4) A & B Domains

Protein crystallography data

The structure of Crystal Structure of the CA2+/Cam Complex with Independent Peptides of KV7.4 (KCNQ4) A & B Domains, PDB code: 6n5w was solved by A.B.Taylor, C.R.Archer, M.S.Shapiro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.28 / 2.15
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 43.510, 130.570, 36.160, 90.00, 90.00, 90.00
R / Rfree (%) 23.3 / 27.4

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the CA2+/Cam Complex with Independent Peptides of KV7.4 (KCNQ4) A & B Domains (pdb code 6n5w). 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 CA2+/Cam Complex with Independent Peptides of KV7.4 (KCNQ4) A & B Domains, PDB code: 6n5w:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 6n5w

Go back to Calcium Binding Sites List in 6n5w
Calcium binding site 1 out of 2 in the Crystal Structure of the CA2+/Cam Complex with Independent Peptides of KV7.4 (KCNQ4) A & B Domains


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 CA2+/Cam Complex with Independent Peptides of KV7.4 (KCNQ4) A & B Domains within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca201

b:51.6
occ:1.00
OD1 C:ASP22 2.2 58.8 1.0
O C:THR26 2.3 46.4 1.0
OE2 C:GLU31 2.4 46.8 1.0
OD1 C:ASP20 2.4 49.6 1.0
OD1 C:ASP24 2.6 58.2 1.0
OE1 C:GLU31 2.7 43.1 1.0
O C:HOH307 2.7 48.4 1.0
CD C:GLU31 2.8 47.2 1.0
CG C:ASP22 3.1 57.2 1.0
CG C:ASP20 3.5 46.2 1.0
CG C:ASP24 3.5 60.9 1.0
C C:THR26 3.5 49.0 1.0
OD2 C:ASP22 3.6 63.0 1.0
OD2 C:ASP24 4.0 61.3 1.0
CA C:ASP20 4.0 41.1 1.0
N C:THR26 4.1 48.9 1.0
CB C:ASP20 4.2 41.3 1.0
CG2 C:THR26 4.2 53.6 1.0
CB C:ASP22 4.2 57.0 1.0
N C:ASP24 4.3 48.7 1.0
CG C:GLU31 4.3 40.8 1.0
OD2 C:ASP20 4.3 46.7 1.0
CA C:THR26 4.4 48.1 1.0
C C:ASP20 4.4 41.7 1.0
N C:ASP22 4.4 54.6 1.0
N C:ILE27 4.5 41.0 1.0
N C:GLY23 4.5 55.9 1.0
CB C:ASP24 4.6 51.7 1.0
CA C:ILE27 4.6 38.8 1.0
O C:HOH304 4.7 47.7 1.0
CA C:ASP22 4.7 54.6 1.0
O C:ASP20 4.7 43.1 1.0
C C:ASP22 4.8 59.1 1.0
N C:LYS21 4.8 46.4 1.0
N C:THR28 4.9 40.3 1.0
CA C:ASP24 4.9 51.9 1.0
N C:GLY25 4.9 43.7 1.0
CB C:THR26 5.0 52.9 1.0
CG2 C:THR28 5.0 41.3 1.0

Calcium binding site 2 out of 2 in 6n5w

Go back to Calcium Binding Sites List in 6n5w
Calcium binding site 2 out of 2 in the Crystal Structure of the CA2+/Cam Complex with Independent Peptides of KV7.4 (KCNQ4) A & B Domains


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 CA2+/Cam Complex with Independent Peptides of KV7.4 (KCNQ4) A & B Domains within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca202

b:45.2
occ:1.00
OD1 C:ASP56 2.4 53.3 1.0
O C:THR62 2.5 41.0 1.0
OD1 C:ASP58 2.5 69.4 1.0
OD1 C:ASN60 2.5 58.9 1.0
OE1 C:GLU67 2.6 44.5 1.0
OE2 C:GLU67 2.7 52.8 1.0
CD C:GLU67 3.0 47.3 1.0
CG C:ASP58 3.5 75.7 1.0
CG C:ASN60 3.5 61.0 1.0
CG C:ASP56 3.6 51.2 1.0
C C:THR62 3.6 43.8 1.0
OD2 C:ASP58 3.8 71.2 1.0
ND2 C:ASN60 4.0 62.5 1.0
N C:ASP64 4.3 44.4 1.0
OD2 C:ASP56 4.3 49.0 1.0
N C:THR62 4.3 48.1 1.0
CA C:ASP56 4.4 46.2 1.0
CA C:ILE63 4.4 35.8 1.0
N C:ILE63 4.4 41.1 1.0
CB C:ASP56 4.5 46.6 1.0
CG C:ASP64 4.5 50.0 1.0
CG C:GLU67 4.5 43.6 1.0
OG1 C:THR62 4.6 55.1 1.0
CA C:THR62 4.6 49.7 1.0
OD2 C:ASP64 4.6 57.5 1.0
N C:ASP58 4.6 66.1 1.0
N C:ASN60 4.6 58.5 1.0
N C:ALA57 4.7 73.0 1.0
OD1 C:ASP64 4.7 48.9 1.0
CB C:ASN60 4.7 59.2 1.0
C C:ASP56 4.7 56.0 1.0
C C:ILE63 4.8 42.5 1.0
CB C:ASP58 4.8 59.7 1.0
N C:GLY61 4.9 52.6 1.0
CB C:ASP64 4.9 46.0 1.0

Reference:

C.R.Archer, B.T.Enslow, A.B.Taylor, V.De La Rosa, A.Bhattacharya, M.S.Shapiro. A Mutually Induced Conformational Fit Underlies CA2+-Directed Interactions Between Calmodulin and the Proximal C Terminus of KCNQ4 K+Channels. J. Biol. Chem. V. 294 6094 2019.
ISSN: ESSN 1083-351X
PubMed: 30808708
DOI: 10.1074/JBC.RA118.006857
Page generated: Tue Jul 16 11:36:18 2024

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