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Zinc in PDB 3ebh: Structure of the M1 Alanylaminopeptidase From Malaria Complexed with Bestatin

Protein crystallography data

The structure of Structure of the M1 Alanylaminopeptidase From Malaria Complexed with Bestatin, PDB code: 3ebh was solved by S.Mcgowan, C.J.Porter, A.M.Buckle, J.C.Whisstock, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.47 / 1.65
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 75.651, 108.628, 117.964, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 20.2

Other elements in 3ebh:

The structure of Structure of the M1 Alanylaminopeptidase From Malaria Complexed with Bestatin also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of the M1 Alanylaminopeptidase From Malaria Complexed with Bestatin (pdb code 3ebh). 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 Structure of the M1 Alanylaminopeptidase From Malaria Complexed with Bestatin, PDB code: 3ebh:

Zinc binding site 1 out of 1 in 3ebh

Go back to Zinc Binding Sites List in 3ebh
Zinc binding site 1 out of 1 in the Structure of the M1 Alanylaminopeptidase From Malaria Complexed with Bestatin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the M1 Alanylaminopeptidase From Malaria Complexed with Bestatin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1

b:10.5
occ:1.00
NE2 A:HIS496 2.0 10.3 1.0
OE1 A:GLU519 2.0 11.9 1.0
NE2 A:HIS500 2.0 9.1 1.0
O2 A:BES1085 2.1 15.3 1.0
O3 A:BES1085 2.5 21.7 1.0
CD A:GLU519 2.8 10.6 1.0
CD2 A:HIS496 2.9 9.7 1.0
CD2 A:HIS500 2.9 9.0 1.0
OE2 A:GLU519 3.0 8.5 1.0
C2 A:BES1085 3.0 17.0 1.0
C3 A:BES1085 3.0 20.6 1.0
CE1 A:HIS496 3.1 12.0 1.0
CE1 A:HIS500 3.1 11.1 1.0
C1 A:BES1085 3.7 14.7 1.0
N2 A:BES1085 3.7 15.0 1.0
OE1 A:GLU497 4.0 10.2 1.0
CG A:HIS496 4.1 9.3 1.0
CG A:HIS500 4.1 9.6 1.0
ND1 A:HIS496 4.1 11.9 1.0
ND1 A:HIS500 4.2 9.4 1.0
OH A:TYR580 4.2 13.8 1.0
N1 A:BES1085 4.2 18.6 1.0
CE1 A:TYR580 4.3 7.9 1.0
CG A:GLU519 4.3 9.8 1.0
OE1 A:GLU463 4.4 13.0 1.0
OE2 A:GLU497 4.5 12.4 1.0
CZ A:TYR580 4.6 11.1 1.0
CD A:GLU497 4.7 10.1 1.0
CG2 A:THR522 4.7 8.8 1.0
CA A:GLU519 4.7 9.3 1.0
OE2 A:GLU463 4.8 14.8 1.0
CD A:GLU463 4.8 15.4 1.0
CB A:GLU519 4.8 9.7 1.0
CB A:THR522 4.8 8.2 1.0
NZ A:LYS518 5.0 14.3 1.0

Reference:

S.Mcgowan, C.J.Porter, J.Lowther, C.M.Stack, S.J.Golding, T.S.Skinner-Adams, K.R.Trenholme, F.Teuscher, S.M.Donnelly, J.Grembecka, A.Mucha, P.Kafarski, R.Degori, A.M.Buckle, D.L.Gardiner, J.C.Whisstock, J.P.Dalton. Structural Basis For the Inhibition of the Essential Plasmodium Falciparum M1 Neutral Aminopeptidase Proc.Natl.Acad.Sci.Usa V. 106 2537 2009.
ISSN: ISSN 0027-8424
PubMed: 19196988
DOI: 10.1073/PNAS.0807398106
Page generated: Wed Dec 16 04:15:31 2020

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