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Zinc in PDB 5hh5: Crystal Structure of B3 Metallo-Beta-Lactamase L1 Complexed with A Phosphonate-Based Inhibitor

Enzymatic activity of Crystal Structure of B3 Metallo-Beta-Lactamase L1 Complexed with A Phosphonate-Based Inhibitor

All present enzymatic activity of Crystal Structure of B3 Metallo-Beta-Lactamase L1 Complexed with A Phosphonate-Based Inhibitor:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of B3 Metallo-Beta-Lactamase L1 Complexed with A Phosphonate-Based Inhibitor, PDB code: 5hh5 was solved by P.Hinchliffe, J.Spencer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 52.63 / 1.80
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 105.256, 105.256, 98.573, 90.00, 90.00, 120.00
R / Rfree (%) 16.3 / 19.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of B3 Metallo-Beta-Lactamase L1 Complexed with A Phosphonate-Based Inhibitor (pdb code 5hh5). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of B3 Metallo-Beta-Lactamase L1 Complexed with A Phosphonate-Based Inhibitor, PDB code: 5hh5:

Zinc binding site 1 out of 1 in 5hh5

Go back to Zinc Binding Sites List in 5hh5
Zinc binding site 1 out of 1 in the Crystal Structure of B3 Metallo-Beta-Lactamase L1 Complexed with A Phosphonate-Based Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of B3 Metallo-Beta-Lactamase L1 Complexed with A Phosphonate-Based Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:20.7
occ:0.90
 O10 A:60M407 1.8 45.1 1.0
ND1 A:HIS118 2.1 18.3 1.0
NE2 A:HIS116 2.1 17.0 1.0
NE2 A:HIS196 2.1 19.7 1.0
O A:HOH501 2.8 59.0 1.0
CD2 A:HIS196 2.9 18.3 1.0
P08 A:60M407 3.0 39.4 1.0
CE1 A:HIS118 3.0 18.6 1.0
CD2 A:HIS116 3.0 17.4 1.0
CE1 A:HIS116 3.1 17.6 1.0
CG A:HIS118 3.1 17.5 1.0
O09 A:60M407 3.2 36.1 1.0
CE1 A:HIS196 3.2 20.2 1.0
CB A:HIS118 3.5 16.8 1.0
H4 A:60M407 3.7 47.5 1.0
O A:HOH578 3.9 44.9 1.0
C07 A:60M407 4.0 39.6 1.0
ND1 A:HIS116 4.1 17.4 1.0
CG A:HIS116 4.1 17.5 1.0
NE2 A:HIS118 4.1 17.8 1.0
CG A:HIS196 4.1 18.3 1.0
O11 A:60M407 4.2 48.1 1.0
CD2 A:HIS118 4.2 16.9 1.0
ND1 A:HIS196 4.3 19.3 1.0
H5 A:60M407 4.3 47.5 1.0
OD1 A:ASP120 4.4 22.0 1.0
CD2 A:HIS121 4.5 21.7 1.0
NE2 A:HIS121 4.6 21.2 1.0
CG2 A:THR197 4.9 17.7 1.0
CA A:HIS118 5.0 16.1 1.0

Reference:

P.Hinchliffe, C.A.Tanner, A.P.Krismanich, G.Labbe, V.J.Goodfellow, L.Marrone, A.Y.Desoky, K.Calvopina, E.E.Whittle, F.Zeng, M.B.Avison, N.C.Bols, S.Siemann, J.Spencer, G.I.Dmitrienko. Structural and Kinetic Studies of the Potent Inhibition of Metallo-Beta-Lactamases By 6-Phosphonomethylpyridine-2-Carboxylates. Biochemistry V. 57 1880 2018.
ISSN: ISSN 1520-4995
PubMed: 29485857
DOI: 10.1021/ACS.BIOCHEM.7B01299
Page generated: Sun Oct 27 17:28:06 2024

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