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Cobalt in PDB 9fxh: Crystal Structure of Cobalt(II)-Substituted Double Mutant Y115E Y117E Human Glutaminyl Cyclase

Enzymatic activity of Crystal Structure of Cobalt(II)-Substituted Double Mutant Y115E Y117E Human Glutaminyl Cyclase

All present enzymatic activity of Crystal Structure of Cobalt(II)-Substituted Double Mutant Y115E Y117E Human Glutaminyl Cyclase:
2.3.2.5;

Protein crystallography data

The structure of Crystal Structure of Cobalt(II)-Substituted Double Mutant Y115E Y117E Human Glutaminyl Cyclase, PDB code: 9fxh was solved by G.Tassone, C.Pozzi, S.Mangani, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 61.76 / 2.30
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 86.185, 149.266, 96.007, 90, 96.87, 90
R / Rfree (%) 20.5 / 25.7

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Crystal Structure of Cobalt(II)-Substituted Double Mutant Y115E Y117E Human Glutaminyl Cyclase (pdb code 9fxh). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 3 binding sites of Cobalt where determined in the Crystal Structure of Cobalt(II)-Substituted Double Mutant Y115E Y117E Human Glutaminyl Cyclase, PDB code: 9fxh:
Jump to Cobalt binding site number: 1; 2; 3;

Cobalt binding site 1 out of 3 in 9fxh

Go back to Cobalt Binding Sites List in 9fxh
Cobalt binding site 1 out of 3 in the Crystal Structure of Cobalt(II)-Substituted Double Mutant Y115E Y117E Human Glutaminyl Cyclase


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of Cobalt(II)-Substituted Double Mutant Y115E Y117E Human Glutaminyl Cyclase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co401

b:24.9
occ:1.00
OE2 A:GLU202 1.7 23.5 1.0
OD2 A:ASP159 2.1 20.4 1.0
NE2 A:HIS330 2.1 25.8 1.0
CD A:GLU202 2.4 21.4 1.0
OE1 A:GLU202 2.6 16.3 1.0
CG A:ASP159 2.8 20.3 1.0
O A:HOH639 2.9 31.8 1.0
OD1 A:ASP159 2.9 22.3 1.0
CD2 A:HIS330 3.0 25.4 1.0
CE1 A:HIS330 3.2 25.1 1.0
O A:HOH515 3.7 24.9 1.0
CG A:GLU202 3.9 21.4 1.0
NE1 A:TRP329 4.2 20.8 1.0
CG A:HIS330 4.2 26.1 1.0
ND1 A:HIS330 4.3 26.8 1.0
CB A:ASP159 4.3 19.8 1.0
OE1 A:GLU201 4.6 29.9 1.0
NE2 A:HIS140 4.8 24.1 1.0
CD A:LYS144 4.8 22.3 1.0
CB A:LYS144 4.8 25.0 1.0
CE2 A:TRP329 4.8 20.5 1.0
CE1 A:HIS140 4.8 24.2 1.0
O A:ASP159 4.9 20.9 1.0
CD1 A:TRP329 4.9 18.8 1.0
CD2 A:LEU249 5.0 16.1 1.0
O A:HOH548 5.0 12.6 1.0

Cobalt binding site 2 out of 3 in 9fxh

Go back to Cobalt Binding Sites List in 9fxh
Cobalt binding site 2 out of 3 in the Crystal Structure of Cobalt(II)-Substituted Double Mutant Y115E Y117E Human Glutaminyl Cyclase


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Crystal Structure of Cobalt(II)-Substituted Double Mutant Y115E Y117E Human Glutaminyl Cyclase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Co401

b:22.0
occ:1.00
OE2 B:GLU202 2.0 23.2 1.0
OD2 B:ASP159 2.0 16.6 1.0
NE2 B:HIS330 2.3 23.9 1.0
CG B:ASP159 2.8 17.3 1.0
CD B:GLU202 2.8 22.4 1.0
O B:HOH697 2.8 38.6 1.0
OD1 B:ASP159 2.9 18.8 1.0
OE1 B:GLU202 2.9 18.2 1.0
CD2 B:HIS330 3.1 25.2 1.0
CE1 B:HIS330 3.5 24.9 1.0
NE1 B:TRP329 3.8 19.8 1.0
O B:HOH514 4.1 37.4 1.0
O B:HOH512 4.1 20.7 1.0
CB B:ASP159 4.2 18.3 1.0
CG B:GLU202 4.2 21.5 1.0
CG B:HIS330 4.3 26.4 1.0
ND1 B:HIS330 4.5 27.0 1.0
CE2 B:TRP329 4.5 19.8 1.0
O B:HOH575 4.6 21.9 1.0
CD2 B:LEU249 4.6 13.4 1.0
CD1 B:TRP329 4.6 19.5 1.0
OE1 B:GLU201 4.6 30.9 1.0
CZ2 B:TRP329 4.7 19.5 1.0
NE2 B:HIS140 4.9 24.3 1.0
O B:ASP159 5.0 23.5 1.0

Cobalt binding site 3 out of 3 in 9fxh

Go back to Cobalt Binding Sites List in 9fxh
Cobalt binding site 3 out of 3 in the Crystal Structure of Cobalt(II)-Substituted Double Mutant Y115E Y117E Human Glutaminyl Cyclase


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 3 of Crystal Structure of Cobalt(II)-Substituted Double Mutant Y115E Y117E Human Glutaminyl Cyclase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Co401

b:25.9
occ:1.00
OE2 C:GLU202 1.7 23.3 1.0
OD2 C:ASP159 1.9 18.6 1.0
NE2 C:HIS330 2.2 29.3 1.0
CD C:GLU202 2.6 23.2 1.0
CG C:ASP159 2.7 18.5 1.0
OD1 C:ASP159 2.8 19.5 1.0
OE1 C:GLU202 2.9 20.9 1.0
CD2 C:HIS330 3.0 27.8 1.0
O C:HOH698 3.1 27.8 1.0
CE1 C:HIS330 3.3 29.1 1.0
O C:HOH523 3.6 29.1 1.0
NE1 C:TRP329 4.0 21.9 1.0
CG C:GLU202 4.0 22.8 1.0
CB C:ASP159 4.1 19.2 1.0
CG C:HIS330 4.3 29.4 1.0
ND1 C:HIS330 4.3 30.7 1.0
O C:HOH516 4.4 19.2 1.0
OE1 C:GLU201 4.7 33.8 1.0
CE2 C:TRP329 4.7 21.6 1.0
CD2 C:LEU249 4.7 14.7 1.0
CD1 C:TRP329 4.8 23.5 1.0
CD C:LYS144 4.8 24.9 1.0
NE2 C:HIS140 4.9 19.5 1.0
CB C:LYS144 4.9 25.6 1.0
O C:ASP159 4.9 25.9 1.0
CE1 C:HIS140 5.0 19.8 1.0
CZ2 C:TRP329 5.0 22.4 1.0

Reference:

G.Tassone, C.Pozzi, S.Mangani. Metal Ion Binding to Human Glutaminyl Cyclase: A Structural Perspective. Int J Mol Sci V. 25 2024.
ISSN: ESSN 1422-0067
PubMed: 39125848
DOI: 10.3390/IJMS25158279
Page generated: Sun Jul 13 22:15:02 2025

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