Cobalt in PDB 6lzc: Crystal Structure of Human Methionine Aminopeptidase (HSMETAP1B) in Complex with Kv-P2-4H-05

All present enzymatic activity of Crystal Structure of Human Methionine Aminopeptidase (HSMETAP1B) in Complex with Kv-P2-4H-05:
3.4.11.18;

The structure of Crystal Structure of Human Methionine Aminopeptidase (HSMETAP1B) in Complex with Kv-P2-4H-05, PDB code: 6lzc was solved by C.B.Sandeep, A.Addlagatta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.53 / 1.35
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	47.552, 77.219, 48.651, 90, 91.55, 90
R / Rfree (%)	16.7 / 19.7

The structure of Crystal Structure of Human Methionine Aminopeptidase (HSMETAP1B) in Complex with Kv-P2-4H-05 also contains other interesting chemical elements:

Sodium	(Na)	1 atom
Magnesium	(Mg)	1 atom

The binding sites of Cobalt atom in the Crystal Structure of Human Methionine Aminopeptidase (HSMETAP1B) in Complex with Kv-P2-4H-05 (pdb code 6lzc). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Crystal Structure of Human Methionine Aminopeptidase (HSMETAP1B) in Complex with Kv-P2-4H-05, PDB code: 6lzc:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Crystal Structure of Human Methionine Aminopeptidase (HSMETAP1B) in Complex with Kv-P2-4H-05


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 Human Methionine Aminopeptidase (HSMETAP1B) in Complex with Kv-P2-4H-05 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co401 b:17.2 occ:1.00 O1 A:EYL403 2.0 17.0 0.8 NE2 A:HIS303 2.0 14.7 1.0 OE2 A:GLU367 2.0 16.1 1.0 OD2 A:ASP240 2.1 14.1 1.0 OE1 A:GLU336 2.2 20.8 1.0 O A:HOH505 2.7 25.1 1.0 N A:EYL403 2.9 28.5 0.8 CE1 A:HIS303 3.0 15.6 1.0 CD A:GLU367 3.0 15.1 1.0 CD2 A:HIS303 3.1 16.1 1.0 CG A:ASP240 3.1 14.6 1.0 CD A:GLU336 3.1 18.0 1.0 CO A:CO402 3.2 14.1 1.0 OE2 A:GLU336 3.3 31.4 1.0 OE1 A:GLU367 3.5 14.4 1.0 OD1 A:ASP240 3.5 13.7 1.0 OG1 A:THR334 3.8 16.3 1.0 C A:EYL403 4.0 36.1 0.8 CG2 A:THR334 4.1 15.7 1.0 O A:EYL403 4.2 35.9 0.8 CG A:HIS303 4.2 15.4 1.0 ND1 A:HIS303 4.2 16.5 1.0 O A:HOH501 4.2 21.6 0.5 CB A:ASP240 4.3 13.4 1.0 CB A:THR334 4.3 15.1 1.0 CG A:GLU367 4.3 15.2 1.0 CG A:GLU336 4.4 17.1 1.0 NE2 A:HIS310 4.6 24.2 1.0 C14 A:EYL403 4.7 43.7 0.8 CB A:GLU336 4.8 16.2 1.0 OD2 A:ASP229 5.0 22.8 1.0

Cobalt binding site 2 out of 2 in the Crystal Structure of Human Methionine Aminopeptidase (HSMETAP1B) in Complex with Kv-P2-4H-05


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 Human Methionine Aminopeptidase (HSMETAP1B) in Complex with Kv-P2-4H-05 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co402 b:14.1 occ:1.00 O1 A:EYL403 1.9 17.0 0.8 OD1 A:ASP240 1.9 13.7 1.0 OD1 A:ASP229 2.0 18.0 1.0 OE1 A:GLU367 2.2 14.4 1.0 O A:HOH501 2.2 21.6 0.5 O A:EYL403 2.3 35.9 0.8 OD2 A:ASP229 2.5 22.8 1.0 CG A:ASP229 2.5 13.7 1.0 N A:EYL403 2.7 28.5 0.8 CG A:ASP240 2.8 14.6 1.0 C A:EYL403 3.0 36.1 0.8 CD A:GLU367 3.0 15.1 1.0 OD2 A:ASP240 3.1 14.1 1.0 CO A:CO401 3.2 17.2 1.0 OE2 A:GLU367 3.3 16.1 1.0 O A:HOH505 3.9 25.1 1.0 OG1 A:THR231 4.0 16.4 1.0 CB A:ASP229 4.1 12.8 1.0 ND2 A:ASN242 4.1 12.8 1.0 CB A:ASP240 4.3 13.4 1.0 O A:LEU241 4.3 11.5 1.0 CG A:GLU367 4.4 15.2 1.0 N A:LEU241 4.4 12.3 1.0 O A:ILE230 4.4 13.7 1.0 O A:HOH617 4.4 26.0 1.0 OE2 A:GLU336 4.5 31.4 1.0 C A:LEU241 4.5 11.5 1.0 C1 A:EYL403 4.6 31.5 0.8 O A:HOH522 4.6 22.5 1.0 C A:ASP240 4.7 12.0 1.0 OE1 A:GLU336 4.7 20.8 1.0 CA A:ASP229 4.8 12.1 1.0 CA A:ASP240 4.8 11.9 1.0 CB A:ASN242 4.8 11.6 1.0 N A:ILE230 4.8 13.1 1.0 CB A:GLU367 4.9 13.3 1.0 CA A:LEU241 4.9 12.5 1.0 CD A:GLU336 4.9 18.0 1.0 C A:ASP229 5.0 11.3 1.0 CG A:ASN242 5.0 12.2 1.0 C A:ILE230 5.0 11.8 1.0

C.B.Sandeep, A.Addlagatta. Crystal Structure of Human Methionine Aminopeptidase (HSMETAP1B) in Complex with An-P2-5H-06 To Be Published.