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Molybdenum in PDB 7l5s: Crystal Structure of Haemophilus Influenzae Mtsz at pH 5.5

Enzymatic activity of Crystal Structure of Haemophilus Influenzae Mtsz at pH 5.5

All present enzymatic activity of Crystal Structure of Haemophilus Influenzae Mtsz at pH 5.5:
1.7.2.3;

Protein crystallography data

The structure of Crystal Structure of Haemophilus Influenzae Mtsz at pH 5.5, PDB code: 7l5s was solved by M.A.Struwe, Z.Luo, U.Kappler, B.Kobe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.86 / 2.09
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 60.47, 100.156, 132.859, 90, 90, 90
R / Rfree (%) 15.1 / 18.2

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Crystal Structure of Haemophilus Influenzae Mtsz at pH 5.5 (pdb code 7l5s). 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 Haemophilus Influenzae Mtsz at pH 5.5, PDB code: 7l5s:

Molybdenum binding site 1 out of 1 in 7l5s

Go back to Molybdenum Binding Sites List in 7l5s
Molybdenum binding site 1 out of 1 in the Crystal Structure of Haemophilus Influenzae Mtsz at pH 5.5


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 Haemophilus Influenzae Mtsz at pH 5.5 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo904

b:25.6
occ:1.00
O A:O901 1.9 34.0 1.0
HB3 A:SER187 2.3 34.8 1.0
S13 A:MGD902 2.3 22.3 1.0
S13 A:MGD903 2.4 20.7 1.0
S12 A:MGD902 2.5 23.9 1.0
S12 A:MGD903 2.5 21.0 1.0
HE1 A:TRP156 3.1 24.6 1.0
CB A:SER187 3.2 29.0 1.0
HH A:TYR154 3.3 37.4 1.0
C13 A:MGD902 3.4 23.2 1.0
C12 A:MGD902 3.4 23.5 1.0
C13 A:MGD903 3.4 19.6 1.0
C12 A:MGD903 3.4 21.4 1.0
HA A:SER187 3.5 27.7 1.0
HB2 A:SER187 3.6 34.8 1.0
HE1 A:HIS692 3.7 28.9 1.0
HE1 A:HIS686 3.7 27.5 1.0
HE2 A:HIS692 3.7 30.7 1.0
NE1 A:TRP156 3.8 20.5 1.0
CA A:SER187 3.8 23.1 1.0
OH A:TYR154 3.8 31.1 1.0
OG A:SER187 4.1 39.9 1.0
HZ2 A:TRP156 4.1 24.5 1.0
N A:SER187 4.1 21.6 1.0
H A:SER187 4.2 25.9 1.0
CE1 A:HIS692 4.2 24.1 1.0
NE2 A:HIS692 4.2 25.6 1.0
CE2 A:TRP156 4.5 22.1 1.0
CE1 A:HIS686 4.6 22.9 1.0
CZ2 A:TRP156 4.6 20.4 1.0
HB2 A:TYR186 4.7 25.1 1.0
C11 A:MGD902 4.7 24.4 1.0
CD1 A:TRP156 4.7 19.5 1.0
H101 A:MGD902 4.7 26.2 1.0
C11 A:MGD903 4.7 23.1 1.0
C14 A:MGD902 4.8 20.7 1.0
C A:TYR186 4.8 23.3 1.0
HD1 A:TRP156 4.8 23.4 1.0
C14 A:MGD903 4.8 24.2 1.0
HG A:SER187 4.8 47.8 0.0
H102 A:MGD903 4.9 24.7 1.0
H15 A:MGD902 4.9 22.4 1.0
HH21 A:ARG366 4.9 22.5 1.0
H15 A:MGD903 4.9 26.9 1.0
HE2 A:TYR154 5.0 32.4 1.0
H11 A:MGD902 5.0 29.3 1.0

Reference:

M.A.Struwe, P.Kalimuthu, Z.Luo, Q.Zhong, D.Ellis, J.Yang, K.C.Khadanand, J.R.Harmer, M.L.Kirk, A.G.Mcewan, B.Clement, P.V.Bernhardt, B.Kobe, U.Kappler. Active Site Architecture Reveals Coordination Sphere Flexibility and Specificity Determinants in A Group of Closely Related Molybdoenzymes J.Biol.Chem. 2021.
ISSN: ESSN 1083-351X
Page generated: Sun Oct 6 16:57:29 2024

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