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Calcium in PDB 3hln: Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds

Enzymatic activity of Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds

All present enzymatic activity of Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds:
3.4.21.92;

Protein crystallography data

The structure of Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds, PDB code: 3hln was solved by M.S.Kimber, A.Y.H.Yu, M.Borg, H.S.Chan, W.A.Houry, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.22 / 3.20
Space group P 32 2 1 1
Cell size a, b, c (Å), α, β, γ (°) 182.299, 182.299, 476.859, 90.00, 90.00, 120.00
R / Rfree (%) 21.3 / 25.3

Calcium Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 13;

Binding sites:

The binding sites of Calcium atom in the Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds (pdb code 3hln). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 13 binding sites of Calcium where determined in the Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds, PDB code: 3hln:
Jump to Calcium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Calcium binding site 1 out of 13 in 3hln

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Calcium binding site 1 out of 13 in the Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds


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Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds within 5.0Å range:
probe atom residue distance (Å) B Occ
T:Ca201

b:0.9
occ:1.00
 OE1 T:GLU151 4.0 0.6 1.0
OE2 T:GLU151 4.7 0.4 1.0
CD T:GLU151 4.8 0.9 1.0

Calcium binding site 2 out of 13 in 3hln

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Calcium binding site 2 out of 13 in the Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds


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Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Ca202

b:0.4
occ:1.00
 OD2 J:ASP86 2.4 0.6 1.0
CG J:ASP86 3.6 0.8 1.0
OD1 J:ASP86 4.3 0.3 1.0
NZ J:LYS110 4.4 0.2 1.0
CB J:ASP86 4.5 0.1 1.0

Calcium binding site 3 out of 13 in 3hln

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Calcium binding site 3 out of 13 in the Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds


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Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Ca203

b:0.6
occ:1.00
 NE2 I:GLN163 2.9 0.8 1.0
OE1 Z:GLU165 3.2 0.9 1.0
OE2 Z:GLU165 3.2 0.4 1.0
O I:GLU162 3.4 0.9 1.0
CD2 Z:LEU161 3.6 0.1 1.0
CD Z:GLU165 3.6 0.5 1.0
C I:GLU162 3.7 0.0 1.0
CG Z:LEU161 3.8 0.3 1.0
CA I:GLN163 3.8 0.5 1.0
N I:GLN163 3.9 0.2 1.0
CD I:GLN163 3.9 0.7 1.0
CB Z:LEU161 4.2 0.3 1.0
CB I:GLU162 4.2 0.3 1.0
CB I:ARG166 4.3 0.4 1.0
CB I:GLN163 4.5 0.3 1.0
OE1 I:GLN163 4.5 0.6 1.0
CA I:GLU162 4.6 0.1 1.0
N Z:GLU162 4.7 0.9 1.0
CG I:ARG166 4.7 0.3 1.0
C Z:LEU161 4.8 0.5 1.0
CG I:GLN163 4.8 0.0 1.0
OG I:SER160 4.9 0.8 1.0
CA Z:GLU162 5.0 0.4 1.0

Calcium binding site 4 out of 13 in 3hln

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Calcium binding site 4 out of 13 in the Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds


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Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Ca204

b:0.9
occ:1.00
 CB I:GLU162 3.4 0.3 1.0
CG I:GLU162 3.4 0.7 1.0
N I:GLU162 3.5 0.7 1.0
CA I:GLU162 4.0 0.1 1.0
CD Z:GLU165 4.1 0.5 1.0
CB I:SER160 4.1 0.6 1.0
CG Z:GLU165 4.2 0.4 1.0
N I:LEU161 4.2 0.9 1.0
NH2 O:ARG140 4.2 0.2 1.0
CB Z:GLU165 4.3 0.5 1.0
OE1 Z:GLU165 4.3 0.9 1.0
OE2 Z:GLU165 4.4 0.4 1.0
C I:LEU161 4.5 0.3 1.0
OG I:SER160 4.5 0.8 1.0
CB I:LEU161 4.6 0.9 1.0
CA I:LEU161 4.7 1.0 1.0
C I:SER160 4.7 0.7 1.0
CA I:SER160 4.9 0.6 1.0
CD I:GLU162 4.9 0.7 1.0
OE2 Z:GLU169 4.9 0.6 1.0
CZ O:ARG140 4.9 0.2 1.0

Calcium binding site 5 out of 13 in 3hln

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Calcium binding site 5 out of 13 in the Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds


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Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 5 of Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds within 5.0Å range:
probe atom residue distance (Å) B Occ
1:Ca205

b:0.2
occ:1.00
 NZ 1:LYS144 3.5 0.8 1.0
OE2 2:GLU178 3.8 0.1 1.0
CD 2:GLU178 4.7 0.9 1.0
CE 1:LYS144 4.7 0.4 1.0

Calcium binding site 6 out of 13 in 3hln

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Calcium binding site 6 out of 13 in the Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 6 of Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Ca206

b:0.5
occ:1.00
 OD1 J:ASP167 3.4 0.2 1.0
O O:GLN159 3.8 0.7 1.0
CZ J:ARG166 4.0 0.5 1.0
NH2 J:ARG166 4.1 0.7 1.0
NH1 J:ARG166 4.1 0.9 1.0
CD2 O:LEU155 4.5 0.2 1.0
CG J:ASP167 4.5 0.3 1.0
O O:ALA154 4.5 0.2 1.0
NE J:ARG166 4.6 0.2 1.0
O J:ARG166 4.6 0.2 1.0
CA J:ASP167 4.6 0.3 1.0
C O:ALA154 4.7 0.2 1.0
CA O:LEU155 4.8 1.0 1.0
CG J:ARG166 4.8 0.3 1.0
N O:LEU155 4.8 0.1 1.0
CB O:ALA154 4.9 0.4 1.0
C O:GLN159 4.9 0.8 1.0
CD1 O:LEU155 5.0 0.6 1.0

Calcium binding site 7 out of 13 in 3hln

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Calcium binding site 7 out of 13 in the Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 7 of Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds within 5.0Å range:
probe atom residue distance (Å) B Occ
Z:Ca215

b:0.1
occ:1.00
 O Z:GLN81 3.4 0.7 1.0
O Z:ILE83 3.6 0.7 1.0
O Z:LYS84 3.8 0.3 1.0
ND1 1:HIS191 4.4 0.6 1.0
C Z:LYS84 4.5 0.3 1.0
C Z:GLN81 4.5 0.5 1.0
C Z:ILE83 4.7 0.6 1.0
CA Z:LYS84 4.8 0.6 1.0
O Z:PRO85 4.8 0.9 1.0
OD1 Z:ASP86 4.8 0.4 1.0
CE1 1:HIS191 4.8 0.8 1.0

Calcium binding site 8 out of 13 in 3hln

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Calcium binding site 8 out of 13 in the Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 8 of Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds within 5.0Å range:
probe atom residue distance (Å) B Occ
2:Ca216

b:0.5
occ:1.00
 OD2 2:ASP86 2.6 0.2 1.0
CG 2:ASP86 3.4 0.5 1.0
OD1 2:ASP86 3.5 0.5 1.0
CB 2:ASP86 4.9 0.0 1.0

Calcium binding site 9 out of 13 in 3hln

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Calcium binding site 9 out of 13 in the Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 9 of Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ca217

b:0.2
occ:1.00
 O E:VAL180 3.9 0.5 1.0
CA E:GLY183 4.6 1.0 1.0
O E:VAL185 4.8 0.2 1.0
O E:ASP186 4.8 0.8 1.0

Calcium binding site 10 out of 13 in 3hln

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Calcium binding site 10 out of 13 in the Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 10 of Crystal Structure of Clpp A153C Mutant with Inter-Heptamer Disulfide Bonds within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ca218

b:0.7
occ:1.00
 O E:ILE83 2.8 0.4 1.0
O E:GLN81 3.0 0.0 1.0
O E:LYS84 3.7 0.5 1.0
O E:MET80 3.8 0.8 1.0
C E:GLN81 3.9 1.0 1.0
O E:PRO85 4.0 0.8 1.0
C E:ILE83 4.0 0.5 1.0
C E:LYS84 4.3 0.3 1.0
CA E:GLN81 4.3 0.8 1.0
ND1 F:HIS191 4.4 0.9 1.0
CE1 F:HIS191 4.5 0.9 1.0
CA E:LYS84 4.7 0.1 1.0
C E:PRO85 4.7 0.8 1.0
C E:PHE82 4.7 0.9 1.0
N E:ILE83 4.8 0.0 1.0
O E:PHE82 4.8 0.1 1.0
C E:MET80 4.8 0.7 1.0
N E:PHE82 4.8 0.3 1.0
N E:LYS84 4.8 0.8 1.0
OD1 E:ASP86 4.8 0.5 1.0

Reference:

M.S.Kimber, A.Y.Yu, M.Borg, E.Leung, H.S.Chan, W.A.Houry. Structural and Theoretical Studies Indicate That the Cylindrical Protease Clpp Samples Extended and Compact Conformations. Structure V. 18 798 2010.
ISSN: ISSN 0969-2126
PubMed: 20637416
DOI: 10.1016/J.STR.2010.04.008
Page generated: Sat Jul 13 11:06:14 2024

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