Atomistry » Cobalt » PDB 1a0c-1e1c » 1boa
Atomistry »
  Cobalt »
    PDB 1a0c-1e1c »
      1boa »

Cobalt in PDB 1boa: Human Methionine Aminopeptidase 2 Complexed with Angiogenesis Inhibitor Fumagillin

Enzymatic activity of Human Methionine Aminopeptidase 2 Complexed with Angiogenesis Inhibitor Fumagillin

All present enzymatic activity of Human Methionine Aminopeptidase 2 Complexed with Angiogenesis Inhibitor Fumagillin:
3.4.11.18;

Protein crystallography data

The structure of Human Methionine Aminopeptidase 2 Complexed with Angiogenesis Inhibitor Fumagillin, PDB code: 1boa was solved by S.Liu, J.Widom, C.W.Kemp, C.M.Crews, J.C.Clardy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 1.80
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 90.700, 99.580, 101.950, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 23.2

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Human Methionine Aminopeptidase 2 Complexed with Angiogenesis Inhibitor Fumagillin (pdb code 1boa). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Human Methionine Aminopeptidase 2 Complexed with Angiogenesis Inhibitor Fumagillin, PDB code: 1boa:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 1boa

Go back to Cobalt Binding Sites List in 1boa
Cobalt binding site 1 out of 2 in the Human Methionine Aminopeptidase 2 Complexed with Angiogenesis Inhibitor Fumagillin


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Human Methionine Aminopeptidase 2 Complexed with Angiogenesis Inhibitor Fumagillin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co481

b:47.9
occ:1.00
OD2 A:ASP262 2.2 27.8 1.0
OE2 A:GLU364 2.3 28.9 1.0
OE2 A:GLU459 2.3 20.3 1.0
O A:HOH662 2.4 34.5 1.0
NE2 A:HIS331 2.5 18.3 1.0
CO A:CO482 3.0 48.3 1.0
CD A:GLU364 3.0 28.1 1.0
CG A:ASP262 3.1 24.3 1.0
OE1 A:GLU364 3.3 26.8 1.0
O11 A:FUG480 3.3 19.4 1.0
CD A:GLU459 3.3 22.5 1.0
CD2 A:HIS331 3.4 16.1 1.0
CE1 A:HIS331 3.5 18.6 1.0
OD1 A:ASP262 3.6 24.0 1.0
OE1 A:GLU459 3.8 21.1 1.0
CB A:ALA362 3.9 18.1 1.0
O A:HOH528 4.0 30.5 1.0
CB A:ASP262 4.1 20.7 1.0
CG A:GLU364 4.3 26.4 1.0
CG A:HIS331 4.6 17.1 1.0
CG A:GLU459 4.6 18.0 1.0
ND1 A:HIS331 4.6 17.7 1.0
C1 A:FUG480 4.6 19.0 1.0
C2A A:FUG480 4.7 17.7 1.0
OD2 A:ASP251 4.8 23.5 1.0
CB A:GLU364 4.9 23.4 1.0

Cobalt binding site 2 out of 2 in 1boa

Go back to Cobalt Binding Sites List in 1boa
Cobalt binding site 2 out of 2 in the Human Methionine Aminopeptidase 2 Complexed with Angiogenesis Inhibitor Fumagillin


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Human Methionine Aminopeptidase 2 Complexed with Angiogenesis Inhibitor Fumagillin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co482

b:48.3
occ:1.00
OD1 A:ASP262 1.9 24.0 1.0
O A:HOH662 2.1 34.5 1.0
OD2 A:ASP251 2.3 23.5 1.0
OD1 A:ASP251 2.3 22.6 1.0
OE1 A:GLU459 2.4 21.1 1.0
CG A:ASP262 2.5 24.3 1.0
OD2 A:ASP262 2.6 27.8 1.0
CG A:ASP251 2.7 21.9 1.0
CO A:CO481 3.0 47.9 1.0
CD A:GLU459 3.1 22.5 1.0
OE2 A:GLU459 3.2 20.3 1.0
O A:HOH528 3.7 30.5 1.0
CB A:ASP262 4.0 20.7 1.0
OE1 A:GLU364 4.0 26.8 1.0
CZ A:PHE219 4.1 15.9 1.0
O A:HOH586 4.1 33.1 1.0
CB A:ASP251 4.2 15.3 1.0
NE2 A:GLN457 4.2 15.8 1.0
CE1 A:PHE219 4.4 14.9 1.0
O A:HOH643 4.4 38.0 1.0
O11 A:FUG480 4.5 19.4 1.0
CA A:ASP262 4.6 18.3 1.0
C A:ASP262 4.6 15.3 1.0
OE2 A:GLU364 4.6 28.9 1.0
CG A:GLU459 4.6 18.0 1.0
N A:CYS263 4.6 12.6 1.0
CB A:ALA264 4.7 12.5 1.0
CD A:GLU364 4.7 28.1 1.0
CE2 A:PHE219 5.0 17.1 1.0
CA A:ASP251 5.0 13.1 1.0

Reference:

S.Liu, J.Widom, C.W.Kemp, C.M.Crews, J.Clardy. Structure of Human Methionine Aminopeptidase-2 Complexed with Fumagillin. Science V. 282 1324 1998.
ISSN: ISSN 0036-8075
PubMed: 9812898
DOI: 10.1126/SCIENCE.282.5392.1324
Page generated: Sun Dec 13 10:34:16 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy