Atomistry » Lead » PDB 3fhh-8gbm » 5b6t
Atomistry »
  Lead »
    PDB 3fhh-8gbm »
      5b6t »

Lead in PDB 5b6t: Catalytic Domain of Coprinopsis Cinerea GH62 Alpha-L- Arabinofuranosidase Complexed with Pb

Enzymatic activity of Catalytic Domain of Coprinopsis Cinerea GH62 Alpha-L- Arabinofuranosidase Complexed with Pb

All present enzymatic activity of Catalytic Domain of Coprinopsis Cinerea GH62 Alpha-L- Arabinofuranosidase Complexed with Pb:
3.2.1.55;

Protein crystallography data

The structure of Catalytic Domain of Coprinopsis Cinerea GH62 Alpha-L- Arabinofuranosidase Complexed with Pb, PDB code: 5b6t was solved by T.Tonozuka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.63 / 1.48
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.854, 77.765, 74.458, 90.00, 93.01, 90.00
R / Rfree (%) 15 / 17.4

Other elements in 5b6t:

The structure of Catalytic Domain of Coprinopsis Cinerea GH62 Alpha-L- Arabinofuranosidase Complexed with Pb also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Lead Binding Sites:

The binding sites of Lead atom in the Catalytic Domain of Coprinopsis Cinerea GH62 Alpha-L- Arabinofuranosidase Complexed with Pb (pdb code 5b6t). This binding sites where shown within 5.0 Angstroms radius around Lead atom.
In total only one binding site of Lead was determined in the Catalytic Domain of Coprinopsis Cinerea GH62 Alpha-L- Arabinofuranosidase Complexed with Pb, PDB code: 5b6t:

Lead binding site 1 out of 1 in 5b6t

Go back to Lead Binding Sites List in 5b6t
Lead binding site 1 out of 1 in the Catalytic Domain of Coprinopsis Cinerea GH62 Alpha-L- Arabinofuranosidase Complexed with Pb


Mono view


Stereo pair view

A full contact list of Lead with other atoms in the Pb binding site number 1 of Catalytic Domain of Coprinopsis Cinerea GH62 Alpha-L- Arabinofuranosidase Complexed with Pb within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pb500

b:31.2
occ:1.00
 O A:HOH768 2.2 15.6 1.0
O2 A:GOL502 2.6 18.0 1.0
O A:HOH717 2.6 25.8 1.0
OE1 A:GLU276 2.6 9.6 1.0
OE2 A:GLU276 2.7 10.8 1.0
CD A:GLU276 3.0 9.6 1.0
OH A:TYR380 3.3 11.7 1.0
C2 A:GOL502 3.7 18.3 1.0
CZ A:TYR380 3.7 11.1 1.0
CE2 A:TYR380 3.9 10.6 1.0
O A:HOH665 4.1 8.9 1.0
O A:HOH631 4.2 8.3 1.0
O A:HOH683 4.4 8.9 1.0
OD2 A:ASP241 4.4 10.3 1.0
CG A:GLU276 4.6 8.7 1.0
C1 A:GOL502 4.6 19.1 1.0
CE1 A:TYR380 4.6 11.3 1.0
CE2 A:PHE275 4.7 9.6 1.0
O A:HOH617 4.7 9.5 1.0
OD1 A:ASP241 4.7 10.4 1.0
NH2 A:ARG302 4.8 9.4 1.0
C3 A:GOL502 4.8 17.5 1.0
CD2 A:TYR380 4.9 11.2 1.0
O1 A:GOL502 4.9 15.6 1.0
NH1 A:ARG302 4.9 8.6 1.0
CG A:ASP241 5.0 10.1 1.0

Reference:

T.Tonozuka, Y.Tanaka, S.Okuyama, T.Miyazaki, A.Nishikawa, M.Yoshida. Structure of the Catalytic Domain of Alpha-L-Arabinofuranosidase From Coprinopsis Cinerea, CCABF62A, Provides Insights Into Structure-Function Relationships in Glycoside Hydrolase Family 62 Appl. Biochem. Biotechnol. V. 181 511 2017.
ISSN: ISSN 1559-0291
PubMed: 27589854
DOI: 10.1007/S12010-016-2227-0
Page generated: Thu Oct 10 10:09:25 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy