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Molybdenum in PDB 2bii: Crystal Structure of Nitrate-Reducing Fragment of Assimilatory Nitrate Reductase From Pichia Angusta

Enzymatic activity of Crystal Structure of Nitrate-Reducing Fragment of Assimilatory Nitrate Reductase From Pichia Angusta

All present enzymatic activity of Crystal Structure of Nitrate-Reducing Fragment of Assimilatory Nitrate Reductase From Pichia Angusta:
1.7.1.2;

Protein crystallography data

The structure of Crystal Structure of Nitrate-Reducing Fragment of Assimilatory Nitrate Reductase From Pichia Angusta, PDB code: 2bii was solved by K.Fischer, G.Barbier, H.-J.Hecht, R.R.Mendel, W.H.Campbell, G.Schwarz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 87.71 / 1.70
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 122.722, 123.080, 149.509, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 21.2

Other elements in 2bii:

The structure of Crystal Structure of Nitrate-Reducing Fragment of Assimilatory Nitrate Reductase From Pichia Angusta also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Crystal Structure of Nitrate-Reducing Fragment of Assimilatory Nitrate Reductase From Pichia Angusta (pdb code 2bii). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Crystal Structure of Nitrate-Reducing Fragment of Assimilatory Nitrate Reductase From Pichia Angusta, PDB code: 2bii:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in 2bii

Go back to Molybdenum Binding Sites List in 2bii
Molybdenum binding site 1 out of 2 in the Crystal Structure of Nitrate-Reducing Fragment of Assimilatory Nitrate Reductase From Pichia Angusta


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Crystal Structure of Nitrate-Reducing Fragment of Assimilatory Nitrate Reductase From Pichia Angusta within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo1479

b:26.0
occ:1.00
MOM1 A:MTV1479 0.0 26.0 1.0
OM1 A:MTV1479 2.0 19.9 1.0
OM2 A:MTV1479 2.1 26.1 1.0
S2' A:MTV1479 2.3 18.6 1.0
S1' A:MTV1479 2.4 22.0 1.0
SG A:CYS139 2.6 23.4 1.0
C2' A:MTV1479 3.3 20.3 1.0
C1' A:MTV1479 3.3 20.2 1.0
N A:ALA140 3.7 15.8 1.0
CB A:CYS139 3.8 17.8 1.0
N A:GLY247 3.8 16.8 1.0
CA A:CYS139 3.9 17.0 1.0
O A:HOH2396 4.2 32.3 1.0
ND2 A:ASN272 4.2 20.6 1.0
CG A:ARG89 4.2 21.0 1.0
C A:CYS139 4.3 15.5 1.0
CA A:GLY247 4.3 18.0 1.0
NE A:ARG89 4.3 20.7 1.0
CD A:ARG89 4.4 23.1 1.0
C A:GLY246 4.5 16.4 1.0
CB A:ALA140 4.6 16.5 1.0
O A:HOH2395 4.6 27.7 1.0
CB A:ARG89 4.7 18.8 1.0
CA A:ALA140 4.7 16.8 1.0
C3' A:MTV1479 4.7 20.3 1.0
C6 A:MTV1479 4.8 21.2 1.0
CA A:GLY246 4.8 17.3 1.0
N A:GLY141 4.9 16.9 1.0
N A:GLY246 4.9 16.2 1.0
OD1 A:ASN272 5.0 24.9 1.0

Molybdenum binding site 2 out of 2 in 2bii

Go back to Molybdenum Binding Sites List in 2bii
Molybdenum binding site 2 out of 2 in the Crystal Structure of Nitrate-Reducing Fragment of Assimilatory Nitrate Reductase From Pichia Angusta


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Crystal Structure of Nitrate-Reducing Fragment of Assimilatory Nitrate Reductase From Pichia Angusta within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mo1479

b:26.1
occ:1.00
MOM1 B:MTV1479 0.0 26.1 1.0
OM1 B:MTV1479 2.0 20.8 1.0
OM2 B:MTV1479 2.1 27.4 1.0
S2' B:MTV1479 2.4 19.4 1.0
S1' B:MTV1479 2.4 21.8 1.0
SG B:CYS139 2.6 22.7 1.0
C2' B:MTV1479 3.3 21.7 1.0
C1' B:MTV1479 3.3 21.3 1.0
CB B:CYS139 3.7 19.3 1.0
N B:ALA140 3.7 17.0 1.0
CA B:CYS139 3.8 17.8 1.0
N B:GLY247 3.9 17.2 1.0
ND2 B:ASN272 4.2 19.4 1.0
C B:CYS139 4.2 16.5 1.0
CG B:ARG89 4.2 21.3 1.0
NE B:ARG89 4.3 23.1 1.0
O B:HOH2186 4.3 37.0 1.0
CA B:GLY247 4.3 17.4 1.0
CD B:ARG89 4.4 22.2 1.0
O B:HOH2399 4.5 27.8 1.0
C B:GLY246 4.5 17.0 1.0
CB B:ALA140 4.6 17.6 1.0
CA B:ALA140 4.7 16.8 1.0
CB B:ARG89 4.7 18.6 1.0
C3' B:MTV1479 4.8 23.2 1.0
CA B:GLY246 4.8 16.9 1.0
C6 B:MTV1479 4.8 21.5 1.0
N B:GLY246 4.9 15.9 1.0
N B:GLY141 4.9 17.5 1.0
OD1 B:ASN272 5.0 24.6 1.0

Reference:

K.Fischer, G.Barbier, H.-J.Hecht, R.R.Mendel, W.H.Campbell, G.Schwarz. Structural Basis of Eukaryotic Nitrate Reduction: Crystal Structures of the Nitrate Reductase Active Site Plant Cell V. 17 1167 2005.
ISSN: ISSN 1040-4651
PubMed: 15772287
DOI: 10.1105/TPC.104.029694
Page generated: Tue Dec 15 05:16:57 2020

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