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Calcium in PDB 1scm: Structure of the Regulatory Domain of Scallop Myosin at 2.8 Angstroms Resolution

Protein crystallography data

The structure of Structure of the Regulatory Domain of Scallop Myosin at 2.8 Angstroms Resolution, PDB code: 1scm was solved by C.Cohen, X.Xie, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 52.500, 87.000, 55.500, 90.00, 114.50, 90.00
R / Rfree (%) 20.1 / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of the Regulatory Domain of Scallop Myosin at 2.8 Angstroms Resolution (pdb code 1scm). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of the Regulatory Domain of Scallop Myosin at 2.8 Angstroms Resolution, PDB code: 1scm:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1scm

Go back to Calcium Binding Sites List in 1scm
Calcium binding site 1 out of 2 in the Structure of the Regulatory Domain of Scallop Myosin at 2.8 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of the Regulatory Domain of Scallop Myosin at 2.8 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca502

b:36.9
occ:1.00
O B:PHE34 2.5 41.5 1.0
OD1 B:ASP32 2.6 43.0 1.0
OD1 B:ASP30 2.7 23.3 1.0
CG B:ASP28 2.8 34.0 1.0
OD1 B:ASP28 2.9 29.9 1.0
OD2 B:ASP28 3.0 36.0 1.0
OD2 B:ASP39 3.1 30.8 1.0
C B:PHE34 3.4 24.9 1.0
CB B:ASP28 3.5 28.0 1.0
N B:PHE34 3.6 24.8 1.0
CG B:ASP32 3.6 43.9 1.0
CG B:ASP39 3.7 38.7 1.0
OD1 B:ASP39 3.8 42.7 1.0
CA B:ASP28 3.8 34.9 1.0
N B:GLY33 3.8 39.7 1.0
CG B:ASP30 3.9 33.3 1.0
OG B:SER36 4.0 58.1 1.0
N B:ASP32 4.0 47.8 1.0
N B:VAL35 4.1 23.7 1.0
CA B:PHE34 4.2 24.9 1.0
OD2 B:ASP32 4.2 55.4 1.0
CA B:VAL35 4.2 25.9 1.0
N B:ARG31 4.3 47.7 1.0
C B:GLY33 4.3 29.4 1.0
N B:ASP30 4.4 43.7 1.0
N B:VAL29 4.4 49.2 1.0
CA B:GLY33 4.5 32.1 1.0
C B:ARG31 4.5 53.1 1.0
C B:ASP28 4.5 41.7 1.0
N B:SER36 4.5 36.7 1.0
CA B:ASP32 4.6 41.7 1.0
C B:ASP32 4.6 41.6 1.0
CB B:ASP32 4.6 39.3 1.0
CA B:ARG31 4.7 54.6 1.0
OD2 B:ASP30 4.7 36.2 1.0
C B:ASP30 4.8 39.2 1.0
CA B:ASP30 4.9 33.7 1.0
CB B:ASP30 4.9 26.5 1.0
CB B:ASP39 4.9 27.2 1.0
C B:VAL35 5.0 30.5 1.0

Calcium binding site 2 out of 2 in 1scm

Go back to Calcium Binding Sites List in 1scm
Calcium binding site 2 out of 2 in the Structure of the Regulatory Domain of Scallop Myosin at 2.8 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of the Regulatory Domain of Scallop Myosin at 2.8 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca501

b:26.7
occ:1.00
O C:ALA27 2.4 14.0 1.0
O C:GLY23 2.5 35.2 1.0
OD1 C:ASP22 2.6 25.6 1.0
OD1 C:ASP19 2.6 13.1 1.0
O C:ASP19 2.7 29.7 1.0
O C:ASP22 2.8 26.0 1.0
OD1 C:ASP25 2.9 41.5 1.0
C C:ASP22 3.5 13.4 1.0
C C:GLY23 3.6 19.7 1.0
C C:ALA27 3.6 10.7 1.0
C C:ASP19 3.6 21.0 1.0
CG C:ASP22 3.7 32.0 1.0
CG C:ASP19 3.7 20.8 1.0
CA C:ASP19 3.8 22.9 1.0
CG C:ASP25 3.8 36.5 1.0
N C:ASP25 4.1 31.3 1.0
N C:ALA27 4.2 15.0 1.0
N C:GLY23 4.2 19.0 1.0
CB C:ASP22 4.2 22.1 1.0
CB C:ASP19 4.3 13.8 1.0
CA C:GLY23 4.3 17.3 1.0
OD2 C:ASP25 4.3 40.8 1.0
CA C:ASP22 4.4 21.5 1.0
CA C:ALA27 4.4 9.0 1.0
CA C:VAL28 4.4 22.6 1.0
N C:VAL28 4.5 15.1 1.0
N C:ARG24 4.5 28.0 1.0
CA C:ARG24 4.6 26.6 1.0
OD2 C:ASP22 4.7 38.9 1.0
N C:ASP22 4.8 23.8 1.0
OD2 C:ASP19 4.8 26.1 1.0
CB C:ALA27 4.8 8.2 1.0
O C:PHE18 4.8 12.2 1.0
CA C:ASP25 4.9 30.3 1.0
C C:ASP25 4.9 28.5 1.0
CB C:ASP25 4.9 26.0 1.0
C C:ARG24 4.9 27.2 1.0
N C:PHE20 4.9 17.8 1.0

Reference:

X.Xie, D.H.Harrison, I.Schlichting, R.M.Sweet, V.N.Kalabokis, A.G.Szent-Gyorgyi, C.Cohen. Structure of the Regulatory Domain of Scallop Myosin at 2.8 A Resolution. Nature V. 368 306 1994.
ISSN: ISSN 0028-0836
PubMed: 8127365
DOI: 10.1038/368306A0
Page generated: Tue Jul 8 01:54:23 2025

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