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Cobalt in PDB 1c24: E. Coli Methionine Aminopeptidase: Methionine Phosphinate Complex

Enzymatic activity of E. Coli Methionine Aminopeptidase: Methionine Phosphinate Complex

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

Protein crystallography data

The structure of E. Coli Methionine Aminopeptidase: Methionine Phosphinate Complex, PDB code: 1c24 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) 24.60 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 39.293, 67.633, 48.865, 90.00, 111.15, 90.00
R / Rfree (%) n/a / n/a

Other elements in 1c24:

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

Sodium (Na) 1 atom

Cobalt Binding Sites:

The binding sites of Cobalt atom in the E. Coli Methionine Aminopeptidase: Methionine Phosphinate Complex (pdb code 1c24). 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: Methionine Phosphinate Complex, PDB code: 1c24:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 1c24

Go back to Cobalt Binding Sites List in 1c24
Cobalt binding site 1 out of 2 in the E. Coli Methionine Aminopeptidase: Methionine Phosphinate 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: Methionine Phosphinate Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co401

b:17.6
occ:0.99
OD1 A:ASP108 1.9 14.0 1.0
O2 A:MPJ300 2.0 13.7 0.6
OE1 A:GLU235 2.1 15.5 1.0
NE2 A:HIS171 2.1 9.6 1.0
O1 A:MPJ300 2.3 29.3 0.7
OE2 A:GLU204 2.4 14.6 1.0
O2 A:MPJ300 2.6 18.7 0.7
P A:MPJ300 2.8 35.5 0.6
CG A:ASP108 2.9 14.7 1.0
P A:MPJ300 2.9 18.7 0.7
CD A:GLU235 3.0 21.1 1.0
CE1 A:HIS171 3.1 18.3 1.0
CD2 A:HIS171 3.1 17.1 1.0
CD A:GLU204 3.2 19.3 1.0
CO A:CO402 3.2 16.1 1.0
OE2 A:GLU235 3.4 14.2 1.0
OE1 A:GLU204 3.4 20.1 1.0
OD2 A:ASP108 3.4 15.3 1.0
OG1 A:THR202 3.9 14.2 1.0
O1 A:MPJ300 3.9 12.4 0.6
N A:MPJ300 4.1 13.3 1.0
CB A:ASP108 4.1 12.5 1.0
CA A:MPJ300 4.1 17.0 1.0
CG2 A:THR202 4.2 11.3 1.0
ND1 A:HIS171 4.3 10.8 1.0
CG A:HIS171 4.3 13.8 1.0
CB A:THR202 4.4 9.9 1.0
CG A:GLU235 4.4 14.3 1.0
CG A:GLU204 4.5 14.1 1.0
NE2 A:HIS178 4.6 22.7 1.0
CE1 A:PHE177 5.0 19.1 1.0
CD2 A:HIS178 5.0 20.1 1.0

Cobalt binding site 2 out of 2 in 1c24

Go back to Cobalt Binding Sites List in 1c24
Cobalt binding site 2 out of 2 in the E. Coli Methionine Aminopeptidase: Methionine Phosphinate 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: Methionine Phosphinate Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co402

b:16.1
occ:0.96
O2 A:MPJ300 2.0 13.7 0.6
OD2 A:ASP108 2.0 15.3 1.0
OE2 A:GLU235 2.1 14.2 1.0
OD1 A:ASP97 2.1 13.8 1.0
N A:MPJ300 2.3 13.3 1.0
O1 A:MPJ300 2.3 29.3 0.7
OD2 A:ASP97 2.4 15.3 1.0
CG A:ASP97 2.5 8.7 1.0
CG A:ASP108 2.9 14.7 1.0
CA A:MPJ300 3.1 17.0 1.0
CD A:GLU235 3.1 21.1 1.0
OD1 A:ASP108 3.1 14.0 1.0
P A:MPJ300 3.1 35.5 0.6
CO A:CO401 3.2 17.6 1.0
P A:MPJ300 3.2 18.7 0.7
OE1 A:GLU235 3.3 15.5 1.0
O A:HOH502 3.9 19.7 1.0
OG1 A:THR99 4.0 15.1 1.0
CB A:ASP97 4.0 9.5 1.0
O2 A:MPJ300 4.1 18.7 0.7
OE1 A:GLU204 4.1 20.1 1.0
O A:HOH570 4.2 33.2 1.0
O1 A:MPJ300 4.3 12.4 0.6
CB A:ASP108 4.3 12.5 1.0
O A:HOH552 4.4 27.0 1.0
CG A:GLU235 4.4 14.3 1.0
N A:THR109 4.5 8.3 1.0
CB A:MPJ300 4.5 21.5 1.0
O A:VAL98 4.7 16.8 1.0
C A:ASP108 4.7 15.8 1.0
O A:THR109 4.7 12.3 1.0
OE2 A:GLU204 4.8 14.6 1.0
CD A:GLU204 4.8 19.3 1.0
CA A:ASP108 4.8 13.5 1.0
CA A:ASP97 4.8 10.5 1.0
C A:THR109 4.9 12.9 1.0
CB A:GLU235 4.9 9.6 1.0
C A:ASP97 5.0 12.6 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 Jul 13 17:24:53 2025

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