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Molybdenum in PDB 2bih: Crystal Structure of the Molybdenum-Containing Nitrate Reducing Fragment of Pichia Angusta Assimilatory Nitrate Reductase

Enzymatic activity of Crystal Structure of the Molybdenum-Containing Nitrate Reducing Fragment of Pichia Angusta Assimilatory Nitrate Reductase

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

Protein crystallography data

The structure of Crystal Structure of the Molybdenum-Containing Nitrate Reducing Fragment of Pichia Angusta Assimilatory Nitrate Reductase, PDB code: 2bih 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) 65.94 / 2.60
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 76.740, 76.740, 306.086, 90.00, 90.00, 120.00
R / Rfree (%) 19 / 25.8

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Crystal Structure of the Molybdenum-Containing Nitrate Reducing Fragment of Pichia Angusta Assimilatory Nitrate Reductase (pdb code 2bih). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total only one binding site of Molybdenum was determined in the Crystal Structure of the Molybdenum-Containing Nitrate Reducing Fragment of Pichia Angusta Assimilatory Nitrate Reductase, PDB code: 2bih:

Molybdenum binding site 1 out of 1 in 2bih

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


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 the Molybdenum-Containing Nitrate Reducing Fragment of Pichia Angusta Assimilatory Nitrate Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo1479

b:57.6
occ:1.00
MOM1 A:MTV1479 0.0 57.6 1.0
OM1 A:MTV1479 2.0 19.9 1.0
OM2 A:MTV1479 2.1 26.1 1.0
S1' A:MTV1479 2.3 48.3 1.0
S2' A:MTV1479 2.4 44.6 1.0
SG A:CYS139 2.7 46.1 1.0
C1' A:MTV1479 3.3 46.4 1.0
C2' A:MTV1479 3.3 46.7 1.0
N A:ALA140 3.7 40.9 1.0
N A:GLY247 3.8 39.3 1.0
CB A:CYS139 3.8 43.7 1.0
CA A:CYS139 3.8 42.8 1.0
CG A:ARG89 4.1 44.9 1.0
OD1 A:ASN272 4.1 43.2 1.0
CA A:GLY247 4.2 39.4 1.0
C A:CYS139 4.3 41.7 1.0
CD A:ARG89 4.4 46.9 1.0
CB A:ALA140 4.4 39.9 1.0
C A:GLY246 4.5 39.4 1.0
NE A:ARG89 4.5 49.1 1.0
CB A:ARG89 4.6 45.4 1.0
CA A:ALA140 4.7 40.8 1.0
CA A:GLY246 4.7 38.9 1.0
C6 A:MTV1479 4.7 44.5 1.0
C3' A:MTV1479 4.8 44.6 1.0
ND2 A:ASN272 4.8 44.5 1.0
N A:GLY246 4.8 38.6 1.0
CG A:ASN272 4.8 44.0 1.0
N A:GLY141 4.9 40.5 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 05:16:55 2020

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