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Manganese in PDB 1jku: Crystal Structure of Manganese Catalase From Lactobacillus Plantarum

Enzymatic activity of Crystal Structure of Manganese Catalase From Lactobacillus Plantarum

All present enzymatic activity of Crystal Structure of Manganese Catalase From Lactobacillus Plantarum:
1.11.1.6;

Protein crystallography data

The structure of Crystal Structure of Manganese Catalase From Lactobacillus Plantarum, PDB code: 1jku was solved by V.V.Barynin, M.M.Whittaker, S.V.Antonyuk, V.S.Lamzin, P.M.Harrison, P.J.Artymiuk, J.W.Whittaker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.94 / 1.84
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 74.720, 96.420, 106.690, 90.00, 106.88, 90.00
R / Rfree (%) 14.5 / 18.7

Other elements in 1jku:

The structure of Crystal Structure of Manganese Catalase From Lactobacillus Plantarum also contains other interesting chemical elements:

Calcium (Ca) 6 atoms

Manganese Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Manganese atom in the Crystal Structure of Manganese Catalase From Lactobacillus Plantarum (pdb code 1jku). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 12 binding sites of Manganese where determined in the Crystal Structure of Manganese Catalase From Lactobacillus Plantarum, PDB code: 1jku:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Manganese binding site 1 out of 12 in 1jku

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Manganese binding site 1 out of 12 in the Crystal Structure of Manganese Catalase From Lactobacillus Plantarum


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Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Manganese Catalase From Lactobacillus Plantarum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1267

b:12.1
occ:1.00
 OE1 A:GLU35 1.8 14.2 1.0
O A:OH1269 1.9 15.4 1.0
O A:OH1270 2.1 17.8 1.0
O A:OH1271 2.1 25.6 1.0
OE1 A:GLU66 2.1 12.1 1.0
ND1 A:HIS69 2.2 14.3 1.0
CD A:GLU35 2.9 14.8 1.0
CE1 A:HIS69 3.0 16.5 1.0
MN A:MN31268 3.0 12.5 1.0
CD A:GLU66 3.1 9.7 1.0
CG A:HIS69 3.3 11.9 1.0
OE2 A:GLU66 3.3 11.2 1.0
OE2 A:GLU35 3.4 18.2 1.0
CB A:HIS69 3.8 10.6 1.0
OE2 A:GLU178 3.9 24.9 1.0
NE2 A:HIS69 4.2 12.9 1.0
CG A:GLU35 4.2 12.5 1.0
NH2 A:ARG147 4.3 13.8 1.0
CD2 A:HIS69 4.4 13.5 1.0
CG A:GLU66 4.5 12.2 1.0
ND1 A:HIS181 4.5 11.8 1.0
CG A:GLU178 4.6 14.3 1.0
CE1 A:HIS181 4.6 11.3 1.0
CD A:GLU178 4.7 22.0 1.0
CA A:GLU66 4.8 10.7 1.0
CD2 A:LEU174 4.8 18.2 1.0
OE1 A:GLU148 4.9 14.4 1.0
CB A:GLU66 4.9 11.3 1.0
CB A:GLU35 4.9 10.7 1.0

Manganese binding site 2 out of 12 in 1jku

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Manganese binding site 2 out of 12 in the Crystal Structure of Manganese Catalase From Lactobacillus Plantarum


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Manganese Catalase From Lactobacillus Plantarum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1268

b:12.5
occ:1.00
 O A:OH1269 2.0 15.4 1.0
OE2 A:GLU66 2.1 11.2 1.0
ND1 A:HIS181 2.2 11.8 1.0
O A:OH1270 2.2 17.8 1.0
OE1 A:GLU148 2.4 14.4 1.0
OE2 A:GLU148 2.4 14.8 1.0
CD A:GLU148 2.7 16.2 1.0
CE1 A:HIS181 3.0 11.3 1.0
MN A:MN31267 3.0 12.1 1.0
CD A:GLU66 3.1 9.7 1.0
CG A:HIS181 3.3 11.3 1.0
OE1 A:GLU66 3.4 12.1 1.0
NH2 A:ARG147 3.5 13.8 1.0
CB A:HIS181 3.7 11.4 1.0
CG A:GLU178 4.0 14.3 1.0
O A:OH1271 4.1 25.6 1.0
NE2 A:HIS181 4.2 11.0 1.0
CG A:GLU148 4.2 13.1 1.0
CD2 A:HIS181 4.3 10.6 1.0
CG A:GLU66 4.4 12.2 1.0
OE1 A:GLU35 4.6 14.2 1.0
ND1 A:HIS69 4.6 14.3 1.0
O A:ARG177 4.6 13.5 1.0
CA A:GLU178 4.6 13.2 1.0
CE1 A:HIS69 4.7 16.5 1.0
OE2 A:GLU178 4.7 24.9 1.0
CZ A:ARG147 4.7 11.5 1.0
OH A:TYR42 4.8 13.8 1.0
CE2 A:TYR42 4.9 11.4 1.0
CD A:GLU178 4.9 22.0 1.0
CG2 A:THR62 4.9 12.8 1.0
C A:ARG177 4.9 13.9 1.0
CB A:GLU178 5.0 12.0 1.0
N A:GLU178 5.0 12.5 1.0

Manganese binding site 3 out of 12 in 1jku

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Manganese binding site 3 out of 12 in the Crystal Structure of Manganese Catalase From Lactobacillus Plantarum


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of Manganese Catalase From Lactobacillus Plantarum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn2267

b:12.6
occ:1.00
 OE1 B:GLU35 1.8 17.0 1.0
O B:OH2269 1.9 15.6 1.0
O B:OH2270 2.0 18.7 1.0
OE1 B:GLU66 2.0 12.2 1.0
ND1 B:HIS69 2.1 12.1 1.0
O B:OH2271 2.1 22.5 1.0
CD B:GLU35 2.9 16.1 1.0
CE1 B:HIS69 3.0 12.5 1.0
CD B:GLU66 3.0 10.4 1.0
MN B:MN32268 3.1 12.9 1.0
OE2 B:GLU35 3.3 20.0 1.0
CG B:HIS69 3.3 13.5 1.0
OE2 B:GLU66 3.3 11.4 1.0
CB B:HIS69 3.8 11.4 1.0
OE2 B:GLU178 3.9 25.4 1.0
NE2 B:HIS69 4.2 14.4 1.0
CG B:GLU35 4.2 13.2 1.0
NH2 B:ARG147 4.3 12.0 1.0
CD2 B:HIS69 4.3 15.0 1.0
CG B:GLU66 4.4 11.3 1.0
CG B:GLU178 4.5 15.7 1.0
ND1 B:HIS181 4.6 11.1 1.0
CE1 B:HIS181 4.6 13.9 1.0
CD B:GLU178 4.6 24.0 1.0
CD2 B:LEU174 4.7 18.4 1.0
CA B:GLU66 4.8 10.9 1.0
OE1 B:GLU148 4.8 13.7 1.0
CB B:GLU66 4.8 10.5 1.0
CB B:GLU35 4.9 10.9 1.0

Manganese binding site 4 out of 12 in 1jku

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Manganese binding site 4 out of 12 in the Crystal Structure of Manganese Catalase From Lactobacillus Plantarum


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of Manganese Catalase From Lactobacillus Plantarum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn2268

b:12.9
occ:1.00
 O B:OH2269 1.9 15.6 1.0
OE2 B:GLU66 2.0 11.4 1.0
O B:OH2270 2.2 18.7 1.0
ND1 B:HIS181 2.2 11.1 1.0
OE1 B:GLU148 2.3 13.7 1.0
OE2 B:GLU148 2.5 16.7 1.0
CD B:GLU148 2.7 16.6 1.0
CD B:GLU66 3.0 10.4 1.0
CE1 B:HIS181 3.0 13.9 1.0
MN B:MN32267 3.1 12.6 1.0
CG B:HIS181 3.3 14.9 1.0
OE1 B:GLU66 3.3 12.2 1.0
NH2 B:ARG147 3.6 12.0 1.0
CB B:HIS181 3.7 14.0 1.0
CG B:GLU178 3.9 15.7 1.0
O B:OH2271 4.1 22.5 1.0
NE2 B:HIS181 4.2 15.1 1.0
CG B:GLU148 4.2 14.2 1.0
CD2 B:HIS181 4.3 13.7 1.0
CG B:GLU66 4.4 11.3 1.0
O B:ARG177 4.6 14.0 1.0
ND1 B:HIS69 4.6 12.1 1.0
CA B:GLU178 4.6 14.6 1.0
OE1 B:GLU35 4.6 17.0 1.0
CE1 B:HIS69 4.7 12.5 1.0
OE2 B:GLU178 4.7 25.4 1.0
CZ B:ARG147 4.7 10.1 1.0
OH B:TYR42 4.8 13.5 1.0
CE2 B:TYR42 4.8 10.6 1.0
CD B:GLU178 4.9 24.0 1.0
C B:ARG177 4.9 14.5 1.0
CB B:GLU178 4.9 15.1 1.0
N B:GLU178 5.0 14.2 1.0
CG2 B:THR62 5.0 13.3 1.0
OE2 B:GLU35 5.0 20.0 1.0

Manganese binding site 5 out of 12 in 1jku

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Manganese binding site 5 out of 12 in the Crystal Structure of Manganese Catalase From Lactobacillus Plantarum


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Crystal Structure of Manganese Catalase From Lactobacillus Plantarum within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn3267

b:13.6
occ:1.00
 O C:OH3269 1.7 23.5 1.0
OE1 C:GLU35 1.9 13.9 1.0
O C:OH3270 2.0 15.7 1.0
OE1 C:GLU66 2.0 14.0 1.0
O C:OH3271 2.1 25.4 1.0
ND1 C:HIS69 2.2 13.6 1.0
CD C:GLU35 3.0 18.0 1.0
CD C:GLU66 3.0 12.1 1.0
MN C:MN33268 3.0 15.7 1.0
CE1 C:HIS69 3.1 14.5 1.0
OE2 C:GLU66 3.3 12.2 1.0
CG C:HIS69 3.3 14.1 1.0
OE2 C:GLU35 3.3 19.0 1.0
CB C:HIS69 3.7 10.1 1.0
OE2 C:GLU178 3.9 22.6 1.0
NH2 C:ARG147 4.2 15.9 1.0
NE2 C:HIS69 4.3 14.8 1.0
CG C:GLU35 4.3 12.4 1.0
CD2 C:HIS69 4.4 15.8 1.0
CG C:GLU66 4.4 11.6 1.0
CG C:GLU178 4.5 13.9 1.0
ND1 C:HIS181 4.7 14.7 1.0
CD C:GLU178 4.7 20.5 1.0
OE1 C:GLU148 4.8 14.0 1.0
CA C:GLU66 4.8 12.3 1.0
CD2 C:LEU174 4.8 20.6 1.0
CE1 C:HIS181 4.8 15.5 1.0
CB C:GLU66 4.8 12.4 1.0
CB C:GLU35 4.9 11.2 1.0

Manganese binding site 6 out of 12 in 1jku

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Manganese binding site 6 out of 12 in the Crystal Structure of Manganese Catalase From Lactobacillus Plantarum


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of Crystal Structure of Manganese Catalase From Lactobacillus Plantarum within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn3268

b:15.7
occ:1.00
 O C:OH3270 1.9 15.7 1.0
O C:OH3269 1.9 23.5 1.0
OE2 C:GLU66 2.1 12.2 1.0
OE1 C:GLU148 2.2 14.0 1.0
ND1 C:HIS181 2.3 14.7 1.0
OE2 C:GLU148 2.4 15.3 1.0
CD C:GLU148 2.7 15.0 1.0
MN C:MN33267 3.0 13.6 1.0
CD C:GLU66 3.0 12.1 1.0
CE1 C:HIS181 3.1 15.5 1.0
OE1 C:GLU66 3.3 14.0 1.0
CG C:HIS181 3.4 13.8 1.0
NH2 C:ARG147 3.5 15.9 1.0
CB C:HIS181 3.8 12.1 1.0
CG C:GLU178 4.0 13.9 1.0
O C:OH3271 4.0 25.4 1.0
CG C:GLU148 4.2 11.0 1.0
NE2 C:HIS181 4.3 16.0 1.0
CG C:GLU66 4.4 11.6 1.0
CD2 C:HIS181 4.4 10.4 1.0
ND1 C:HIS69 4.6 13.6 1.0
O C:ARG177 4.6 14.2 1.0
CA C:GLU178 4.6 12.6 1.0
CE1 C:HIS69 4.7 14.5 1.0
CZ C:ARG147 4.7 15.8 1.0
OE1 C:GLU35 4.7 13.9 1.0
OE2 C:GLU178 4.8 22.6 1.0
OH C:TYR42 4.9 15.5 1.0
CB C:GLU178 4.9 12.4 1.0
CE2 C:TYR42 4.9 13.1 1.0
C C:ARG177 4.9 14.3 1.0
CG2 C:THR62 4.9 14.3 1.0
CD C:GLU178 4.9 20.5 1.0
N C:GLU178 5.0 14.1 1.0

Manganese binding site 7 out of 12 in 1jku

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Manganese binding site 7 out of 12 in the Crystal Structure of Manganese Catalase From Lactobacillus Plantarum


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 7 of Crystal Structure of Manganese Catalase From Lactobacillus Plantarum within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn4267

b:12.2
occ:1.00
 O D:OH4270 1.7 17.0 1.0
OE1 D:GLU35 1.9 16.8 1.0
O D:OH4269 2.0 15.5 1.0
OE1 D:GLU66 2.0 13.7 1.0
O D:OH4271 2.1 24.4 1.0
ND1 D:HIS69 2.2 11.4 1.0
CD D:GLU35 3.0 16.8 1.0
CE1 D:HIS69 3.0 12.3 1.0
CD D:GLU66 3.0 13.2 1.0
MN D:MN34268 3.0 13.9 1.0
OE2 D:GLU66 3.2 11.6 1.0
CG D:HIS69 3.3 10.1 1.0
OE2 D:GLU35 3.4 17.4 1.0
CB D:HIS69 3.8 10.3 1.0
OE2 D:GLU178 3.8 25.9 1.0
NH2 D:ARG147 4.2 15.8 1.0
NE2 D:HIS69 4.2 12.9 1.0
CG D:GLU35 4.3 13.4 1.0
CD2 D:HIS69 4.4 9.6 1.0
CG D:GLU178 4.4 13.9 1.0
CG D:GLU66 4.5 12.1 1.0
ND1 D:HIS181 4.5 10.8 1.0
CE1 D:HIS181 4.6 12.1 1.0
CD D:GLU178 4.6 21.7 1.0
OE1 D:GLU148 4.7 16.8 1.0
CD2 D:LEU174 4.8 18.5 1.0
CA D:GLU66 4.8 10.7 1.0
CB D:GLU66 4.9 12.7 1.0
CB D:GLU35 5.0 9.5 1.0

Manganese binding site 8 out of 12 in 1jku

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Manganese binding site 8 out of 12 in the Crystal Structure of Manganese Catalase From Lactobacillus Plantarum


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 8 of Crystal Structure of Manganese Catalase From Lactobacillus Plantarum within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn4268

b:13.9
occ:1.00
 O D:OH4269 1.7 15.5 1.0
OE2 D:GLU66 2.0 11.6 1.0
O D:OH4270 2.1 17.0 1.0
ND1 D:HIS181 2.2 10.8 1.0
OE1 D:GLU148 2.2 16.8 1.0
OE2 D:GLU148 2.4 15.3 1.0
CD D:GLU148 2.6 13.1 1.0
CE1 D:HIS181 3.0 12.1 1.0
MN D:MN34267 3.0 12.2 1.0
CD D:GLU66 3.0 13.2 1.0
CG D:HIS181 3.3 13.0 1.0
OE1 D:GLU66 3.3 13.7 1.0
NH2 D:ARG147 3.5 15.8 1.0
CB D:HIS181 3.7 13.4 1.0
CG D:GLU178 3.9 13.9 1.0
O D:OH4271 4.0 24.4 1.0
CG D:GLU148 4.2 11.8 1.0
NE2 D:HIS181 4.2 13.0 1.0
CD2 D:HIS181 4.3 9.1 1.0
CG D:GLU66 4.4 12.1 1.0
O D:ARG177 4.6 11.9 1.0
CA D:GLU178 4.6 14.2 1.0
OE1 D:GLU35 4.6 16.8 1.0
ND1 D:HIS69 4.6 11.4 1.0
OE2 D:GLU178 4.7 25.9 1.0
CZ D:ARG147 4.7 16.3 1.0
CE1 D:HIS69 4.7 12.3 1.0
OH D:TYR42 4.8 13.7 1.0
CD D:GLU178 4.8 21.7 1.0
CB D:GLU178 4.9 14.0 1.0
CE2 D:TYR42 4.9 9.7 1.0
CG2 D:THR62 4.9 10.9 1.0
C D:ARG177 4.9 13.3 1.0
N D:GLU178 5.0 13.4 1.0

Manganese binding site 9 out of 12 in 1jku

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Manganese binding site 9 out of 12 in the Crystal Structure of Manganese Catalase From Lactobacillus Plantarum


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 9 of Crystal Structure of Manganese Catalase From Lactobacillus Plantarum within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mn5267

b:13.7
occ:1.00
 O E:OH5270 1.9 14.3 1.0
OE1 E:GLU35 1.9 16.9 1.0
O E:OH5269 1.9 20.1 1.0
O E:OH5271 2.1 23.8 1.0
OE1 E:GLU66 2.1 12.8 1.0
ND1 E:HIS69 2.2 13.9 1.0
CD E:GLU35 2.9 16.8 1.0
CD E:GLU66 3.0 11.3 1.0
MN E:MN35268 3.0 14.3 1.0
CE1 E:HIS69 3.1 16.6 1.0
OE2 E:GLU66 3.2 13.5 1.0
OE2 E:GLU35 3.3 16.9 1.0
CG E:HIS69 3.3 13.7 1.0
CB E:HIS69 3.8 13.8 1.0
OE2 E:GLU178 3.8 23.6 1.0
NH2 E:ARG147 4.2 16.8 1.0
NE2 E:HIS69 4.2 15.8 1.0
CG E:GLU35 4.2 11.7 1.0
CD2 E:HIS69 4.4 17.1 1.0
CG E:GLU178 4.4 16.6 1.0
CG E:GLU66 4.4 11.7 1.0
CD E:GLU178 4.6 22.4 1.0
ND1 E:HIS181 4.6 13.1 1.0
CE1 E:HIS181 4.7 14.5 1.0
CD2 E:LEU174 4.7 20.7 1.0
OE1 E:GLU148 4.8 14.6 1.0
CB E:GLU66 4.8 10.8 1.0
CA E:GLU66 4.8 12.4 1.0
CB E:GLU35 4.9 10.1 1.0
OE2 E:GLU148 5.0 15.3 1.0

Manganese binding site 10 out of 12 in 1jku

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Manganese binding site 10 out of 12 in the Crystal Structure of Manganese Catalase From Lactobacillus Plantarum


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 10 of Crystal Structure of Manganese Catalase From Lactobacillus Plantarum within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mn5268

b:14.3
occ:1.00
 O E:OH5269 1.7 20.1 1.0
OE2 E:GLU66 2.0 13.5 1.0
O E:OH5270 2.2 14.3 1.0
ND1 E:HIS181 2.2 13.1 1.0
OE1 E:GLU148 2.3 14.6 1.0
OE2 E:GLU148 2.3 15.3 1.0
CD E:GLU148 2.6 12.9 1.0
CE1 E:HIS181 3.0 14.5 1.0
MN E:MN35267 3.0 13.7 1.0
CD E:GLU66 3.0 11.3 1.0
CG E:HIS181 3.3 13.4 1.0
OE1 E:GLU66 3.4 12.8 1.0
NH2 E:ARG147 3.6 16.8 1.0
CB E:HIS181 3.8 13.3 1.0
CG E:GLU178 3.9 16.6 1.0
O E:OH5271 4.0 23.8 1.0
CG E:GLU148 4.2 11.2 1.0
NE2 E:HIS181 4.2 12.3 1.0
CD2 E:HIS181 4.4 14.3 1.0
CG E:GLU66 4.4 11.7 1.0
O E:ARG177 4.6 14.2 1.0
CA E:GLU178 4.6 14.6 1.0
ND1 E:HIS69 4.7 13.9 1.0
OE1 E:GLU35 4.7 16.9 1.0
CZ E:ARG147 4.7 16.2 1.0
OE2 E:GLU178 4.7 23.6 1.0
CE1 E:HIS69 4.8 16.6 1.0
CB E:GLU178 4.9 15.5 1.0
CE2 E:TYR42 4.9 10.5 1.0
CD E:GLU178 4.9 22.4 1.0
OH E:TYR42 4.9 14.1 1.0
C E:ARG177 4.9 14.2 1.0
CG2 E:THR62 4.9 14.1 1.0
N E:GLU178 4.9 14.8 1.0
OE2 E:GLU35 4.9 16.9 1.0
CB E:GLU148 5.0 9.6 1.0

Reference:

V.V.Barynin, M.M.Whittaker, S.V.Antonyuk, V.S.Lamzin, P.M.Harrison, P.J.Artymiuk, J.W.Whittaker. Crystal Structure of Manganese Catalase From Lactobacillus Plantarum. Structure V. 9 725 2001.
ISSN: ISSN 0969-2126
PubMed: 11587647
DOI: 10.1016/S0969-2126(01)00628-1
Page generated: Tue Dec 15 03:51:06 2020

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