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Manganese in PDB 1hto: Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis

Enzymatic activity of Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis

All present enzymatic activity of Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis:
6.3.1.2;

Protein crystallography data

The structure of Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis, PDB code: 1hto was solved by H.S.Gill, D.Eisenberg, Tb Structural Genomics Consortium (Tbsgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 207.720, 257.690, 274.500, 90.00, 90.00, 90.00
R / Rfree (%) 22.7 / 25.5

Manganese Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 24;

Binding sites:

The binding sites of Manganese atom in the Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis (pdb code 1hto). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 24 binding sites of Manganese where determined in the Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis, PDB code: 1hto:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Manganese binding site 1 out of 24 in 1hto

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Manganese binding site 1 out of 24 in the Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis


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Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn470

b:61.0
occ:0.50
OE1 A:GLU357 2.6 37.9 1.0
ND1 A:HIS269 2.6 44.6 1.0
OE2 A:GLU129 2.8 47.4 1.0
O3P A:AMP7475 3.3 72.1 0.3
CE1 A:HIS269 3.5 37.4 1.0
CG A:HIS269 3.6 25.7 1.0
CD A:GLU357 3.6 32.6 1.0
NH2 A:ARG359 3.7 28.4 1.0
CB A:HIS269 3.8 22.1 1.0
OE2 A:GLU357 4.0 42.2 1.0
CD A:GLU129 4.0 59.3 1.0
NE2 A:HIS271 4.2 43.1 1.0
P A:AMP7475 4.5 83.9 0.3
O1P A:AMP7475 4.5 61.1 0.3
NH1 A:ARG344 4.6 57.4 1.0
OE1 A:GLU129 4.6 79.5 1.0
NE2 A:HIS269 4.6 41.8 1.0
CD2 A:HIS269 4.7 30.1 1.0
CZ A:ARG359 4.8 34.2 1.0
CG A:GLU357 4.8 31.2 1.0
CE1 A:HIS271 4.8 38.0 1.0
O5' A:AMP7475 5.0 71.2 0.3

Manganese binding site 2 out of 24 in 1hto

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Manganese binding site 2 out of 24 in the Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis


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Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn470

b:61.0
occ:0.50
OE1 B:GLU357 2.6 37.9 1.0
ND1 B:HIS269 2.6 44.6 1.0
OE2 B:GLU129 2.8 47.4 1.0
O3P B:AMP7477 3.3 72.1 0.3
CE1 B:HIS269 3.5 37.4 1.0
CG B:HIS269 3.6 25.7 1.0
CD B:GLU357 3.6 32.6 1.0
NH2 B:ARG359 3.7 28.4 1.0
CB B:HIS269 3.8 22.1 1.0
OE2 B:GLU357 4.0 42.2 1.0
CD B:GLU129 4.0 59.3 1.0
NE2 B:HIS271 4.2 43.1 1.0
P B:AMP7477 4.5 83.9 0.3
O1P B:AMP7477 4.5 61.1 0.3
NH1 B:ARG344 4.6 57.4 1.0
OE1 B:GLU129 4.6 79.5 1.0
NE2 B:HIS269 4.6 41.8 1.0
CD2 B:HIS269 4.7 30.1 1.0
CZ B:ARG359 4.8 34.2 1.0
CG B:GLU357 4.8 31.2 1.0
CE1 B:HIS271 4.8 38.0 1.0
O5' B:AMP7477 5.0 71.2 0.3

Manganese binding site 3 out of 24 in 1hto

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Manganese binding site 3 out of 24 in the Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis


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Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn470

b:61.0
occ:0.50
OE1 C:GLU357 2.6 37.9 1.0
ND1 C:HIS269 2.6 44.6 1.0
OE2 C:GLU129 2.8 47.4 1.0
O3P C:AMP7479 3.3 72.1 0.3
CE1 C:HIS269 3.5 37.4 1.0
CG C:HIS269 3.6 25.7 1.0
CD C:GLU357 3.6 32.6 1.0
NH2 C:ARG359 3.7 28.4 1.0
CB C:HIS269 3.8 22.1 1.0
OE2 C:GLU357 4.0 42.2 1.0
CD C:GLU129 4.0 59.3 1.0
NE2 C:HIS271 4.2 43.1 1.0
P C:AMP7479 4.5 83.9 0.3
O1P C:AMP7479 4.5 61.1 0.3
NH1 C:ARG344 4.6 57.4 1.0
OE1 C:GLU129 4.6 79.5 1.0
NE2 C:HIS269 4.6 41.8 1.0
CD2 C:HIS269 4.7 30.1 1.0
CZ C:ARG359 4.8 34.2 1.0
CG C:GLU357 4.8 31.2 1.0
CE1 C:HIS271 4.8 38.0 1.0
O5' C:AMP7479 5.0 71.2 0.3

Manganese binding site 4 out of 24 in 1hto

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Manganese binding site 4 out of 24 in the Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis


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Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn470

b:61.0
occ:0.50
OE1 D:GLU357 2.6 37.9 1.0
ND1 D:HIS269 2.6 44.6 1.0
OE2 D:GLU129 2.8 47.4 1.0
O3P D:AMP7481 3.3 72.1 0.3
CE1 D:HIS269 3.5 37.4 1.0
CG D:HIS269 3.6 25.7 1.0
CD D:GLU357 3.6 32.6 1.0
NH2 D:ARG359 3.7 28.4 1.0
CB D:HIS269 3.8 22.1 1.0
OE2 D:GLU357 4.0 42.2 1.0
CD D:GLU129 4.0 59.3 1.0
NE2 D:HIS271 4.2 43.1 1.0
P D:AMP7481 4.5 83.9 0.3
O1P D:AMP7481 4.5 61.1 0.3
NH1 D:ARG344 4.6 57.4 1.0
OE1 D:GLU129 4.6 79.5 1.0
NE2 D:HIS269 4.6 41.8 1.0
CD2 D:HIS269 4.7 30.1 1.0
CZ D:ARG359 4.8 34.2 1.0
CG D:GLU357 4.8 31.2 1.0
CE1 D:HIS271 4.8 38.0 1.0
O5' D:AMP7481 5.0 71.2 0.3

Manganese binding site 5 out of 24 in 1hto

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Manganese binding site 5 out of 24 in the Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis


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Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mn470

b:61.0
occ:0.50
OE1 E:GLU357 2.6 37.9 1.0
ND1 E:HIS269 2.6 44.6 1.0
OE2 E:GLU129 2.8 47.4 1.0
O3P E:AMP7483 3.3 72.1 0.3
CE1 E:HIS269 3.5 37.4 1.0
CG E:HIS269 3.6 25.7 1.0
CD E:GLU357 3.6 32.6 1.0
NH2 E:ARG359 3.7 28.4 1.0
CB E:HIS269 3.8 22.1 1.0
CD E:GLU129 4.0 59.3 1.0
OE2 E:GLU357 4.0 42.2 1.0
NE2 E:HIS271 4.2 43.1 1.0
P E:AMP7483 4.5 83.9 0.3
O1P E:AMP7483 4.5 61.1 0.3
NH1 E:ARG344 4.6 57.4 1.0
OE1 E:GLU129 4.6 79.5 1.0
NE2 E:HIS269 4.6 41.8 1.0
CD2 E:HIS269 4.7 30.1 1.0
CZ E:ARG359 4.8 34.2 1.0
CG E:GLU357 4.8 31.2 1.0
CE1 E:HIS271 4.8 38.0 1.0
O5' E:AMP7483 5.0 71.2 0.3

Manganese binding site 6 out of 24 in 1hto

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Manganese binding site 6 out of 24 in the Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mn470

b:61.0
occ:0.50
OE1 F:GLU357 2.6 37.9 1.0
ND1 F:HIS269 2.6 44.6 1.0
OE2 F:GLU129 2.8 47.4 1.0
O3P F:AMP7485 3.3 72.1 0.3
CE1 F:HIS269 3.5 37.4 1.0
CG F:HIS269 3.6 25.7 1.0
CD F:GLU357 3.6 32.6 1.0
NH2 F:ARG359 3.7 28.4 1.0
CB F:HIS269 3.8 22.1 1.0
OE2 F:GLU357 4.0 42.2 1.0
CD F:GLU129 4.0 59.3 1.0
NE2 F:HIS271 4.2 43.1 1.0
P F:AMP7485 4.5 83.9 0.3
O1P F:AMP7485 4.5 61.1 0.3
NH1 F:ARG344 4.6 57.4 1.0
OE1 F:GLU129 4.6 79.5 1.0
NE2 F:HIS269 4.6 41.8 1.0
CD2 F:HIS269 4.7 30.1 1.0
CZ F:ARG359 4.8 34.2 1.0
CG F:GLU357 4.8 31.2 1.0
CE1 F:HIS271 4.8 38.0 1.0
O5' F:AMP7485 5.0 71.2 0.3

Manganese binding site 7 out of 24 in 1hto

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Manganese binding site 7 out of 24 in the Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 7 of Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Mn470

b:61.0
occ:0.50
OE1 G:GLU357 2.6 37.9 1.0
ND1 G:HIS269 2.6 44.6 1.0
OE2 G:GLU129 2.8 47.4 1.0
O3P G:AMP7487 3.3 72.1 0.3
CE1 G:HIS269 3.5 37.4 1.0
CG G:HIS269 3.6 25.7 1.0
CD G:GLU357 3.6 32.6 1.0
NH2 G:ARG359 3.7 28.4 1.0
CB G:HIS269 3.8 22.1 1.0
OE2 G:GLU357 4.0 42.2 1.0
CD G:GLU129 4.0 59.3 1.0
NE2 G:HIS271 4.2 43.1 1.0
P G:AMP7487 4.5 83.9 0.3
O1P G:AMP7487 4.5 61.1 0.3
NH1 G:ARG344 4.6 57.4 1.0
OE1 G:GLU129 4.6 79.5 1.0
NE2 G:HIS269 4.6 41.8 1.0
CD2 G:HIS269 4.7 30.1 1.0
CZ G:ARG359 4.8 34.2 1.0
CG G:GLU357 4.8 31.2 1.0
CE1 G:HIS271 4.8 38.0 1.0
O5' G:AMP7487 5.0 71.2 0.3

Manganese binding site 8 out of 24 in 1hto

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Manganese binding site 8 out of 24 in the Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis


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Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 8 of Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Mn470

b:61.0
occ:0.50
OE1 H:GLU357 2.6 37.9 1.0
ND1 H:HIS269 2.6 44.6 1.0
OE2 H:GLU129 2.8 47.4 1.0
O3P H:AMP7489 3.3 72.1 0.3
CE1 H:HIS269 3.5 37.4 1.0
CG H:HIS269 3.6 25.7 1.0
CD H:GLU357 3.6 32.6 1.0
NH2 H:ARG359 3.7 28.4 1.0
CB H:HIS269 3.8 22.1 1.0
OE2 H:GLU357 4.0 42.2 1.0
CD H:GLU129 4.0 59.3 1.0
NE2 H:HIS271 4.2 43.1 1.0
P H:AMP7489 4.5 83.9 0.3
O1P H:AMP7489 4.5 61.1 0.3
NH1 H:ARG344 4.6 57.4 1.0
OE1 H:GLU129 4.6 79.5 1.0
NE2 H:HIS269 4.6 41.8 1.0
CD2 H:HIS269 4.7 30.1 1.0
CZ H:ARG359 4.8 34.2 1.0
CG H:GLU357 4.8 31.2 1.0
CE1 H:HIS271 4.8 38.0 1.0
O5' H:AMP7489 5.0 71.2 0.3

Manganese binding site 9 out of 24 in 1hto

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Manganese binding site 9 out of 24 in the Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 9 of Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Mn470

b:61.0
occ:0.50
OE1 I:GLU357 2.6 37.9 1.0
ND1 I:HIS269 2.6 44.6 1.0
OE2 I:GLU129 2.8 47.4 1.0
O3P I:AMP7491 3.3 72.1 0.3
CE1 I:HIS269 3.5 37.4 1.0
CG I:HIS269 3.6 25.7 1.0
CD I:GLU357 3.6 32.6 1.0
NH2 I:ARG359 3.7 28.4 1.0
CB I:HIS269 3.8 22.1 1.0
OE2 I:GLU357 4.0 42.2 1.0
CD I:GLU129 4.0 59.3 1.0
NE2 I:HIS271 4.2 43.1 1.0
P I:AMP7491 4.5 83.9 0.3
O1P I:AMP7491 4.5 61.1 0.3
NH1 I:ARG344 4.6 57.4 1.0
OE1 I:GLU129 4.6 79.5 1.0
NE2 I:HIS269 4.6 41.8 1.0
CD2 I:HIS269 4.7 30.1 1.0
CZ I:ARG359 4.8 34.2 1.0
CG I:GLU357 4.8 31.2 1.0
CE1 I:HIS271 4.8 38.0 1.0
O5' I:AMP7491 5.0 71.2 0.3

Manganese binding site 10 out of 24 in 1hto

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Manganese binding site 10 out of 24 in the Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 10 of Crystallographic Structure of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Mn470

b:61.0
occ:0.50
OE1 J:GLU357 2.6 37.9 1.0
ND1 J:HIS269 2.6 44.6 1.0
OE2 J:GLU129 2.8 47.4 1.0
O3P J:AMP7493 3.3 72.1 0.3
CE1 J:HIS269 3.5 37.4 1.0
CG J:HIS269 3.6 25.7 1.0
CD J:GLU357 3.6 32.6 1.0
NH2 J:ARG359 3.7 28.4 1.0
CB J:HIS269 3.8 22.1 1.0
CD J:GLU129 4.0 59.3 1.0
OE2 J:GLU357 4.0 42.2 1.0
NE2 J:HIS271 4.2 43.1 1.0
P J:AMP7493 4.5 83.9 0.3
O1P J:AMP7493 4.5 61.1 0.3
NH1 J:ARG344 4.6 57.4 1.0
OE1 J:GLU129 4.6 79.5 1.0
NE2 J:HIS269 4.6 41.8 1.0
CD2 J:HIS269 4.7 30.1 1.0
CZ J:ARG359 4.8 34.2 1.0
CG J:GLU357 4.8 31.2 1.0
CE1 J:HIS271 4.8 38.0 1.0
O5' J:AMP7493 5.0 71.2 0.3

Reference:

H.S.Gill, G.M.Pfluegl, D.Eisenberg. Multicopy Crystallographic Refinement of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis Highlights Flexible Loops in the Enzymatic Mechanism and Its Regulation. Biochemistry V. 41 9863 2002.
ISSN: ISSN 0006-2960
PubMed: 12146952
DOI: 10.1021/BI020254S
Page generated: Tue Dec 15 03:49:16 2020

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