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Manganese in PDB 2vqa: Protein-Folding Location Can Regulate Mn Versus Cu- or Zn- Binding. Crystal Structure of Mnca.

Protein crystallography data

The structure of Protein-Folding Location Can Regulate Mn Versus Cu- or Zn- Binding. Crystal Structure of Mnca., PDB code: 2vqa was solved by S.Tottey, K.J.Waldron, S.J.Firbank, B.Reale, C.Bessant, K.Sato, J.Gray, M.J.Banfield, C.Dennison, N.J.Robinson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 58.32 / 2.95
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 236.190, 236.190, 134.041, 90.00, 90.00, 120.00
R / Rfree (%) 19.1 / 23.3

Manganese Binding Sites:

The binding sites of Manganese atom in the Protein-Folding Location Can Regulate Mn Versus Cu- or Zn- Binding. Crystal Structure of Mnca. (pdb code 2vqa). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 6 binding sites of Manganese where determined in the Protein-Folding Location Can Regulate Mn Versus Cu- or Zn- Binding. Crystal Structure of Mnca., PDB code: 2vqa:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6;

Manganese binding site 1 out of 6 in 2vqa

Go back to Manganese Binding Sites List in 2vqa
Manganese binding site 1 out of 6 in the Protein-Folding Location Can Regulate Mn Versus Cu- or Zn- Binding. Crystal Structure of Mnca.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Protein-Folding Location Can Regulate Mn Versus Cu- or Zn- Binding. Crystal Structure of Mnca. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1005

b:12.4
occ:1.00
OE1 A:GLU108 1.9 12.4 1.0
NE2 A:HIS101 2.2 12.4 1.0
O A:HOH2014 2.2 12.4 1.0
NE2 A:HIS147 2.3 12.4 1.0
NE2 A:HIS103 2.4 12.4 1.0
CE1 A:HIS101 3.0 12.4 1.0
CD A:GLU108 3.0 12.4 1.0
CD2 A:HIS147 3.3 12.4 1.0
CD2 A:HIS101 3.3 12.4 1.0
CE1 A:HIS103 3.3 12.4 1.0
CE1 A:HIS147 3.3 12.4 1.0
CD2 A:HIS103 3.3 12.4 1.0
OE2 A:GLU108 3.4 12.4 1.0
ND1 A:HIS101 4.1 12.4 1.0
CG A:HIS101 4.3 12.4 1.0
CG A:GLU108 4.3 12.4 1.0
CG A:HIS147 4.4 12.4 1.0
ND1 A:HIS147 4.4 12.4 1.0
ND1 A:HIS103 4.4 12.4 1.0
CG A:HIS103 4.5 12.4 1.0
CE1 A:PHE163 4.5 12.4 1.0
CZ A:PHE163 4.7 12.4 1.0
OE2 A:GLU170 4.7 12.4 1.0
CB A:GLU108 4.8 12.4 1.0
CD2 A:PHE141 4.8 12.4 1.0

Manganese binding site 2 out of 6 in 2vqa

Go back to Manganese Binding Sites List in 2vqa
Manganese binding site 2 out of 6 in the Protein-Folding Location Can Regulate Mn Versus Cu- or Zn- Binding. Crystal Structure of Mnca.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Protein-Folding Location Can Regulate Mn Versus Cu- or Zn- Binding. Crystal Structure of Mnca. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1006

b:12.4
occ:1.00
OE1 A:GLU290 2.0 12.4 1.0
NE2 A:HIS283 2.2 12.4 1.0
O A:ACT1395 2.3 12.4 1.0
NE2 A:HIS285 2.3 12.4 1.0
NE2 A:HIS329 2.4 12.4 1.0
CD A:GLU290 2.9 12.4 1.0
OE2 A:GLU290 3.0 12.4 1.0
CE1 A:HIS283 3.1 12.4 1.0
CE1 A:HIS285 3.2 12.4 1.0
CE1 A:HIS329 3.3 12.4 1.0
C A:ACT1395 3.3 12.4 1.0
CD2 A:HIS283 3.3 12.4 1.0
CD2 A:HIS329 3.3 12.4 1.0
CD2 A:HIS285 3.3 12.4 1.0
OXT A:ACT1395 3.6 12.4 1.0
ND1 A:HIS283 4.3 12.4 1.0
CG A:GLU290 4.3 12.4 1.0
ND1 A:HIS285 4.3 12.4 1.0
ND1 A:HIS329 4.4 12.4 1.0
CG A:HIS283 4.4 12.4 1.0
CG A:HIS329 4.4 12.4 1.0
CG A:HIS285 4.4 12.4 1.0
CE1 A:PHE345 4.5 12.4 1.0
CH3 A:ACT1395 4.6 12.4 1.0
CZ A:PHE345 4.6 12.4 1.0
CB A:GLU290 4.8 12.4 1.0
NH1 A:ARG280 4.8 12.4 1.0

Manganese binding site 3 out of 6 in 2vqa

Go back to Manganese Binding Sites List in 2vqa
Manganese binding site 3 out of 6 in the Protein-Folding Location Can Regulate Mn Versus Cu- or Zn- Binding. Crystal Structure of Mnca.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Protein-Folding Location Can Regulate Mn Versus Cu- or Zn- Binding. Crystal Structure of Mnca. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn1001

b:12.4
occ:1.00
OE1 B:GLU108 2.1 12.4 1.0
O B:HOH2008 2.1 12.4 1.0
NE2 B:HIS101 2.2 12.4 1.0
NE2 B:HIS147 2.4 12.4 1.0
NE2 B:HIS103 2.4 12.4 1.0
CE1 B:HIS101 3.0 12.4 1.0
CD B:GLU108 3.0 12.4 1.0
CD2 B:HIS147 3.1 12.4 1.0
OE2 B:GLU108 3.2 12.4 1.0
CE1 B:HIS103 3.2 12.4 1.0
CD2 B:HIS101 3.2 12.4 1.0
CD2 B:HIS103 3.5 12.4 1.0
CE1 B:HIS147 3.5 12.4 1.0
ND1 B:HIS101 4.2 12.4 1.0
CG B:HIS101 4.3 12.4 1.0
CG B:HIS147 4.4 12.4 1.0
ND1 B:HIS103 4.4 12.4 1.0
CG B:GLU108 4.4 12.4 1.0
CE1 B:PHE163 4.5 12.4 1.0
ND1 B:HIS147 4.5 12.4 1.0
CG B:HIS103 4.5 12.4 1.0
OE2 B:GLU170 4.6 12.4 1.0
CZ B:PHE163 4.7 12.4 1.0
CB B:GLU108 4.9 12.4 1.0
CD2 B:PHE141 4.9 12.4 1.0

Manganese binding site 4 out of 6 in 2vqa

Go back to Manganese Binding Sites List in 2vqa
Manganese binding site 4 out of 6 in the Protein-Folding Location Can Regulate Mn Versus Cu- or Zn- Binding. Crystal Structure of Mnca.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Protein-Folding Location Can Regulate Mn Versus Cu- or Zn- Binding. Crystal Structure of Mnca. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn1002

b:12.4
occ:1.00
OE1 B:GLU290 2.0 12.4 1.0
O B:ACT1395 2.3 12.4 1.0
NE2 B:HIS285 2.3 12.4 1.0
NE2 B:HIS283 2.3 12.4 1.0
NE2 B:HIS329 2.4 12.4 1.0
CD B:GLU290 3.0 12.4 1.0
CE1 B:HIS285 3.1 12.4 1.0
CE1 B:HIS283 3.1 12.4 1.0
C B:ACT1395 3.2 12.4 1.0
OE2 B:GLU290 3.2 12.4 1.0
CE1 B:HIS329 3.3 12.4 1.0
CD2 B:HIS283 3.3 12.4 1.0
CD2 B:HIS329 3.3 12.4 1.0
CD2 B:HIS285 3.3 12.4 1.0
OXT B:ACT1395 3.3 12.4 1.0
ND1 B:HIS285 4.3 12.4 1.0
ND1 B:HIS283 4.3 12.4 1.0
CZ B:PHE345 4.3 12.4 1.0
CG B:GLU290 4.4 12.4 1.0
CG B:HIS283 4.4 12.4 1.0
ND1 B:HIS329 4.4 12.4 1.0
CG B:HIS285 4.4 12.4 1.0
CG B:HIS329 4.5 12.4 1.0
CE1 B:PHE345 4.5 12.4 1.0
CH3 B:ACT1395 4.5 12.4 1.0
NH2 B:ARG280 4.7 12.4 1.0
CB B:GLU290 4.8 12.4 1.0

Manganese binding site 5 out of 6 in 2vqa

Go back to Manganese Binding Sites List in 2vqa
Manganese binding site 5 out of 6 in the Protein-Folding Location Can Regulate Mn Versus Cu- or Zn- Binding. Crystal Structure of Mnca.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Protein-Folding Location Can Regulate Mn Versus Cu- or Zn- Binding. Crystal Structure of Mnca. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn1003

b:12.4
occ:1.00
OE1 C:GLU108 1.8 12.4 1.0
O C:HOH2010 2.1 12.4 1.0
NE2 C:HIS101 2.2 12.4 1.0
NE2 C:HIS147 2.3 12.4 1.0
NE2 C:HIS103 2.4 12.4 1.0
CD C:GLU108 2.8 12.4 1.0
CE1 C:HIS101 3.0 12.4 1.0
CD2 C:HIS147 3.1 12.4 1.0
OE2 C:GLU108 3.2 12.4 1.0
CD2 C:HIS101 3.3 12.4 1.0
CE1 C:HIS147 3.3 12.4 1.0
CE1 C:HIS103 3.4 12.4 1.0
CD2 C:HIS103 3.4 12.4 1.0
ND1 C:HIS101 4.2 12.4 1.0
CG C:GLU108 4.2 12.4 1.0
CG C:HIS147 4.3 12.4 1.0
CG C:HIS101 4.4 12.4 1.0
ND1 C:HIS147 4.4 12.4 1.0
OE1 C:GLU170 4.4 12.4 1.0
ND1 C:HIS103 4.5 12.4 1.0
CG C:HIS103 4.5 12.4 1.0
CE1 C:PHE163 4.6 12.4 1.0
CB C:GLU108 4.7 12.4 1.0
CZ C:PHE163 4.8 12.4 1.0
CD2 C:PHE141 5.0 12.4 1.0

Manganese binding site 6 out of 6 in 2vqa

Go back to Manganese Binding Sites List in 2vqa
Manganese binding site 6 out of 6 in the Protein-Folding Location Can Regulate Mn Versus Cu- or Zn- Binding. Crystal Structure of Mnca.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of Protein-Folding Location Can Regulate Mn Versus Cu- or Zn- Binding. Crystal Structure of Mnca. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn1004

b:12.4
occ:1.00
OE1 C:GLU290 2.1 12.4 1.0
NE2 C:HIS283 2.2 12.4 1.0
NE2 C:HIS285 2.3 12.4 1.0
NE2 C:HIS329 2.3 12.4 1.0
OXT C:ACT1393 2.5 12.4 1.0
CD C:GLU290 3.0 12.4 1.0
CE1 C:HIS283 3.0 12.4 1.0
OE2 C:GLU290 3.1 12.4 1.0
CE1 C:HIS329 3.2 12.4 1.0
CE1 C:HIS285 3.2 12.4 1.0
O C:ACT1393 3.2 12.4 1.0
C C:ACT1393 3.3 12.4 1.0
CD2 C:HIS285 3.3 12.4 1.0
CD2 C:HIS329 3.3 12.4 1.0
CD2 C:HIS283 3.4 12.4 1.0
ND1 C:HIS283 4.2 12.4 1.0
ND1 C:HIS329 4.3 12.4 1.0
ND1 C:HIS285 4.4 12.4 1.0
CG C:GLU290 4.4 12.4 1.0
CG C:HIS329 4.4 12.4 1.0
CG C:HIS283 4.4 12.4 1.0
CG C:HIS285 4.4 12.4 1.0
CE1 C:PHE345 4.5 12.4 1.0
CZ C:PHE345 4.5 12.4 1.0
NH2 C:ARG280 4.7 12.4 1.0
CH3 C:ACT1393 4.7 12.4 1.0
CB C:GLU290 4.9 12.4 1.0

Reference:

S.Tottey, K.J.Waldron, S.J.Firbank, B.Reale, C.Bessant, K.Sato, T.R.Cheek, J.Gray, M.J.Banfield, C.Dennison, N.J.Robinson. Protein-Folding Location Can Regulate Manganese-Binding Versus Copper- or Zinc-Binding. Nature V. 455 1138 2008.
ISSN: ISSN 0028-0836
PubMed: 18948958
DOI: 10.1038/NATURE07340
Page generated: Tue Dec 15 04:05:56 2020

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