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Calcium in PDB 7riz: Crystal Structure of RPA3624, A Beta-Propeller Lactonase From Rhodopseudomonas Palustris, with Active-Site Bound 2-Hydroxyquinoline

Enzymatic activity of Crystal Structure of RPA3624, A Beta-Propeller Lactonase From Rhodopseudomonas Palustris, with Active-Site Bound 2-Hydroxyquinoline

All present enzymatic activity of Crystal Structure of RPA3624, A Beta-Propeller Lactonase From Rhodopseudomonas Palustris, with Active-Site Bound 2-Hydroxyquinoline:
3.1.1.17;

Protein crystallography data

The structure of Crystal Structure of RPA3624, A Beta-Propeller Lactonase From Rhodopseudomonas Palustris, with Active-Site Bound 2-Hydroxyquinoline, PDB code: 7riz was solved by C.A.Bingman, B.W.Hall, R.W.Smith, B.G.Fox, T.J.Donohue, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.19 / 1.71
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 48.558, 48.558, 199.122, 90, 90, 120
R / Rfree (%) 17.7 / 21

Other elements in 7riz:

The structure of Crystal Structure of RPA3624, A Beta-Propeller Lactonase From Rhodopseudomonas Palustris, with Active-Site Bound 2-Hydroxyquinoline also contains other interesting chemical elements:

Sodium (Na) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of RPA3624, A Beta-Propeller Lactonase From Rhodopseudomonas Palustris, with Active-Site Bound 2-Hydroxyquinoline (pdb code 7riz). 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 Crystal Structure of RPA3624, A Beta-Propeller Lactonase From Rhodopseudomonas Palustris, with Active-Site Bound 2-Hydroxyquinoline, PDB code: 7riz:

Calcium binding site 1 out of 1 in 7riz

Go back to Calcium Binding Sites List in 7riz
Calcium binding site 1 out of 1 in the Crystal Structure of RPA3624, A Beta-Propeller Lactonase From Rhodopseudomonas Palustris, with Active-Site Bound 2-Hydroxyquinoline


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of RPA3624, A Beta-Propeller Lactonase From Rhodopseudomonas Palustris, with Active-Site Bound 2-Hydroxyquinoline within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca402

b:26.8
occ:1.00
O A:HOH552 2.3 22.6 1.0
OE2 A:GLU15 2.4 31.4 1.0
OD1 A:ASN172 2.4 27.2 1.0
OD1 A:ASN123 2.4 24.0 1.0
OG A:SER230 2.4 27.8 1.0
O1 A:OCH401 2.5 29.2 1.0
OD1 A:ASP229 2.5 32.3 1.0
HD21 A:ASN123 3.2 31.4 1.0
CD A:GLU15 3.4 33.4 1.0
CG A:ASN123 3.4 26.6 1.0
HD22 A:ASN55 3.4 29.4 1.0
CG A:ASN172 3.4 28.5 1.0
HD21 A:ASN172 3.5 31.5 1.0
CB A:SER230 3.5 26.4 1.0
HB2 A:SER230 3.5 31.7 1.0
C1 A:OCH401 3.5 35.1 1.0
HN2 A:OCH401 3.6 51.8 1.0
ND2 A:ASN123 3.6 26.1 1.0
OE1 A:GLU15 3.7 26.8 1.0
CG A:ASP229 3.7 38.4 1.0
HB2 A:ASP124 3.8 27.4 1.0
ND2 A:ASN172 3.9 26.2 1.0
ND2 A:ASN55 3.9 24.5 1.0
HD21 A:ASN55 3.9 29.4 1.0
H A:SER230 4.0 30.9 1.0
N2 A:OCH401 4.0 43.2 1.0
N A:SER230 4.0 25.7 1.0
CA A:SER230 4.2 26.9 1.0
HA A:SER230 4.2 32.2 1.0
HB3 A:SER230 4.3 31.7 1.0
OD2 A:ASP229 4.4 43.1 1.0
O A:THR270 4.4 26.6 1.0
HD22 A:ASN271 4.4 32.8 1.0
C A:ASP229 4.5 27.6 1.0
HD22 A:ASN123 4.5 31.4 1.0
OD2 A:ASP124 4.5 30.3 1.0
HG3 A:GLU15 4.7 38.7 1.0
HA A:ASN172 4.7 30.9 1.0
HA A:ASP229 4.7 30.9 1.0
CG A:GLU15 4.7 32.3 1.0
O A:ASN123 4.7 23.5 1.0
C10 A:OCH401 4.7 39.7 1.0
CB A:ASP124 4.7 22.8 1.0
HB A:THR270 4.7 37.8 1.0
HD22 A:ASN172 4.7 31.5 1.0
CB A:ASN172 4.7 27.9 1.0
CB A:ASN123 4.8 27.1 1.0
ND2 A:ASN271 4.8 27.3 1.0
CB A:ASP229 4.8 27.5 1.0
H10 A:OCH401 4.8 47.7 1.0
C A:ASN172 4.9 26.4 1.0
O A:ASN55 4.9 24.6 1.0
CA A:ASP229 4.9 25.7 1.0
CG A:ASN55 4.9 27.5 1.0
HD21 A:ASN271 4.9 32.8 1.0
CG A:ASP124 4.9 33.1 1.0
C A:ASN123 5.0 24.5 1.0
HB3 A:ASN123 5.0 32.5 1.0

Reference:

B.W.Hall, C.A.Bingman, B.G.Fox, D.R.Noguera, T.J.Donohue. A Broad Specificity Beta-Propeller Enzyme From Rhodopseudomonas Palustris That Hydrolyzes Many Lactones Including Gamma-Valerolactone. J.Biol.Chem. 02782 2022.
ISSN: ESSN 1083-351X
PubMed: 36502920
DOI: 10.1016/J.JBC.2022.102782
Page generated: Thu Jul 10 00:48:40 2025

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