Atomistry » Calcium » PDB 1dva-1edh » 1e3a
Atomistry »
  Calcium »
    PDB 1dva-1edh »
      1e3a »

Calcium in PDB 1e3a: A Slow Processing Precursor Penicillin Acylase From Escherichia Coli

Enzymatic activity of A Slow Processing Precursor Penicillin Acylase From Escherichia Coli

All present enzymatic activity of A Slow Processing Precursor Penicillin Acylase From Escherichia Coli:
3.5.1.11;

Protein crystallography data

The structure of A Slow Processing Precursor Penicillin Acylase From Escherichia Coli, PDB code: 1e3a was solved by L.Hewitt, V.Kasche, K.Lummer, R.J.Lewis, G.N.Murshudov, C.S.Verma, G.G.Dodson, K.S.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 50.710, 64.270, 72.000, 66.14, 74.18, 74.23
R / Rfree (%) 15.8 / 19.7

Other elements in 1e3a:

The structure of A Slow Processing Precursor Penicillin Acylase From Escherichia Coli also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the A Slow Processing Precursor Penicillin Acylase From Escherichia Coli (pdb code 1e3a). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the A Slow Processing Precursor Penicillin Acylase From Escherichia Coli, PDB code: 1e3a:

Calcium binding site 1 out of 1 in 1e3a

Go back to Calcium Binding Sites List in 1e3a
Calcium binding site 1 out of 1 in the A Slow Processing Precursor Penicillin Acylase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of A Slow Processing Precursor Penicillin Acylase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca901

b:8.3
occ:1.00
 OE2 A:GLU152 2.4 8.0 1.0
OD2 B:ASP515 2.5 6.4 1.0
OD1 B:ASP339 2.5 7.4 1.0
O B:PRO468 2.5 5.3 1.0
OD2 B:ASP336 2.6 7.1 1.0
OD1 B:ASP336 2.6 5.6 1.0
O B:VAL338 2.6 6.9 1.0
CG B:ASP336 2.9 6.2 1.0
CG B:ASP515 3.5 8.3 1.0
CD A:GLU152 3.6 8.5 1.0
C B:VAL338 3.6 7.8 1.0
CG B:ASP339 3.6 8.5 1.0
C B:PRO468 3.7 6.7 1.0
CA B:ASP339 3.8 7.8 1.0
CB B:ASP515 3.8 7.4 1.0
NH2 B:ARG462 4.0 7.7 1.0
CG A:GLU152 4.1 7.4 1.0
O B:HOH2413 4.1 7.8 1.0
N B:ASP339 4.1 8.2 1.0
CB B:ASP339 4.2 8.0 1.0
O A:HOH2214 4.2 7.5 1.0
CA B:PRO468 4.2 8.6 1.0
CB B:PRO468 4.2 9.3 1.0
CB B:ASP336 4.4 6.8 1.0
OG1 A:THR150 4.5 7.2 1.0
OE1 A:GLU152 4.6 7.0 1.0
OD1 B:ASP515 4.6 7.0 1.0
OD2 B:ASP339 4.6 7.5 1.0
N B:ARG469 4.7 8.0 1.0
N B:VAL338 4.7 6.6 1.0
CA B:VAL338 4.7 7.7 1.0
O B:HOH2250 4.8 23.1 1.0
CA B:ARG469 4.9 7.0 1.0

Reference:

L.Hewitt, V.Kasche, K.Lummer, R.J.Lewis, G.N.Murshudov, C.S.Verma, G.G.Dodson, K.S.Wilson. Structure of A Slow Processing Precursor Penicillin Acylase From Escherichia Coli Reveals the Linker Peptide Blocking the Active-Site Cleft J.Mol.Biol. V. 302 887 2000.
ISSN: ISSN 0022-2836
PubMed: 10993730
DOI: 10.1006/JMBI.2000.4105
Page generated: Thu Jul 11 07:44:24 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy