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Cobalt in PDB 1c22: E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex

Enzymatic activity of E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex

All present enzymatic activity of E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex:
3.4.11.18;

Protein crystallography data

The structure of E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex, PDB code: 1c22 was solved by W.T.Lowther, Y.Zhang, P.B.Sampson, J.F.Honek, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.10 / 1.75
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 39.128, 67.604, 48.826, 90.00, 111.05, 90.00
R / Rfree (%) n/a / n/a

Other elements in 1c22:

The structure of E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex also contains other interesting chemical elements:

Fluorine (F) 3 atoms
Sodium (Na) 1 atom

Cobalt Binding Sites:

The binding sites of Cobalt atom in the E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex (pdb code 1c22). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex, PDB code: 1c22:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 1c22

Go back to Cobalt Binding Sites List in 1c22
Cobalt binding site 1 out of 2 in the E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co401

b:15.5
occ:1.00
OD1 A:ASP108 2.0 13.6 1.0
O A:MF3300 2.0 12.6 1.0
OE1 A:GLU235 2.0 14.1 1.0
OE2 A:GLU204 2.1 12.3 1.0
NE2 A:HIS171 2.1 9.9 1.0
C A:MF3300 2.8 20.6 1.0
CG A:ASP108 3.0 15.4 1.0
CD A:GLU235 3.0 21.0 1.0
CD A:GLU204 3.0 17.4 1.0
CD2 A:HIS171 3.1 12.0 1.0
CE1 A:HIS171 3.1 14.3 1.0
OXT A:MF3300 3.2 15.7 1.0
OE1 A:GLU204 3.3 19.9 1.0
OE2 A:GLU235 3.4 13.7 1.0
CO A:CO402 3.4 15.1 1.0
OD2 A:ASP108 3.5 12.7 1.0
OG1 A:THR202 3.6 11.7 1.0
CG2 A:THR202 3.9 10.1 1.0
CB A:THR202 4.1 8.9 1.0
CA A:MF3300 4.2 13.8 1.0
CB A:ASP108 4.2 11.0 1.0
CG A:HIS171 4.3 9.8 1.0
ND1 A:HIS171 4.3 11.2 1.0
CG A:GLU204 4.3 14.7 1.0
CG A:GLU235 4.4 13.3 1.0
N A:MF3300 4.5 9.9 1.0
O A:HOH603 4.7 45.0 1.0
NE2 A:HIS178 4.8 20.2 1.0
CB A:GLU204 4.9 10.9 1.0

Cobalt binding site 2 out of 2 in 1c22

Go back to Cobalt Binding Sites List in 1c22
Cobalt binding site 2 out of 2 in the E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co402

b:15.1
occ:1.00
OD2 A:ASP108 2.0 12.7 1.0
OE2 A:GLU235 2.1 13.7 1.0
OD1 A:ASP97 2.1 11.8 1.0
O A:MF3300 2.2 12.6 1.0
N A:MF3300 2.3 9.9 1.0
OD2 A:ASP97 2.3 12.5 1.0
CG A:ASP97 2.5 6.4 1.0
CA A:MF3300 2.9 13.8 1.0
C A:MF3300 2.9 20.6 1.0
CG A:ASP108 3.0 15.4 1.0
CD A:GLU235 3.1 21.0 1.0
OD1 A:ASP108 3.2 13.6 1.0
OE1 A:GLU235 3.4 14.1 1.0
CO A:CO401 3.4 15.5 1.0
O A:HOH504 3.8 13.8 1.0
OG1 A:THR99 3.9 14.2 1.0
CB A:ASP97 4.0 7.1 1.0
OXT A:MF3300 4.1 15.7 1.0
CB A:ASP108 4.3 11.0 1.0
N A:THR109 4.3 7.4 1.0
CB A:MF3300 4.4 20.4 1.0
CG A:GLU235 4.4 13.3 1.0
O A:HOH570 4.4 30.7 1.0
O A:HOH603 4.5 45.0 1.0
O A:VAL98 4.5 14.1 1.0
OE1 A:GLU204 4.6 19.9 1.0
O A:THR109 4.6 11.4 1.0
O A:HOH557 4.6 16.8 1.0
C A:ASP108 4.6 15.0 1.0
CA A:ASP108 4.7 9.9 1.0
OE2 A:GLU204 4.8 12.3 1.0
C A:THR109 4.8 9.5 1.0
CA A:ASP97 4.8 7.6 1.0
N A:VAL98 4.9 8.4 1.0
CB A:GLU235 4.9 6.7 1.0
CA A:THR109 4.9 5.2 1.0
C A:ASP97 4.9 11.0 1.0

Reference:

W.T.Lowther, Y.Zhang, P.B.Sampson, J.F.Honek, B.W.Matthews. Insights Into the Mechanism of Escherichia Coli Methionine Aminopeptidase From the Structural Analysis of Reaction Products and Phosphorus-Based Transition-State Analogues. Biochemistry V. 38 14810 1999.
ISSN: ISSN 0006-2960
PubMed: 10555963
DOI: 10.1021/BI991711G
Page generated: Sun Dec 13 10:34:18 2020

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