Cobalt in PDB 6lzb: Crystal Structure of Human Methionine Aminopeptidase (HSMETAP1B) in Complex with An-P2-5H-06

All present enzymatic activity of Crystal Structure of Human Methionine Aminopeptidase (HSMETAP1B) in Complex with An-P2-5H-06:
3.4.11.18;

The structure of Crystal Structure of Human Methionine Aminopeptidase (HSMETAP1B) in Complex with An-P2-5H-06, PDB code: 6lzb 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)	40.53 / 1.29
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	47.573, 77.251, 48.623, 90, 91.54, 90
R / Rfree (%)	16.3 / 20

The structure of Crystal Structure of Human Methionine Aminopeptidase (HSMETAP1B) in Complex with An-P2-5H-06 also contains other interesting chemical elements:

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

The binding sites of Cobalt atom in the Crystal Structure of Human Methionine Aminopeptidase (HSMETAP1B) in Complex with An-P2-5H-06 (pdb code 6lzb). 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 An-P2-5H-06, PDB code: 6lzb:
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 An-P2-5H-06


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 An-P2-5H-06 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co401 b:16.1 occ:1.00 O1 A:EYF403 1.9 16.6 0.8 NE2 A:HIS303 2.0 14.2 1.0 OE2 A:GLU367 2.0 15.3 1.0 OD2 A:ASP240 2.1 13.3 1.0 OE1 A:GLU336 2.2 19.5 1.0 O A:EYF403 2.6 24.5 0.8 CD A:GLU367 3.0 13.1 1.0 CE1 A:HIS303 3.0 16.4 1.0 CG A:ASP240 3.1 12.9 1.0 CD2 A:HIS303 3.1 14.9 1.0 N A:EYF403 3.1 35.1 0.8 CD A:GLU336 3.1 17.6 1.0 CO A:CO402 3.2 12.8 1.0 OE2 A:GLU336 3.4 31.2 1.0 C A:EYF403 3.4 29.1 0.8 OE1 A:GLU367 3.4 13.4 1.0 OD1 A:ASP240 3.5 12.5 1.0 OG1 A:THR334 3.8 15.1 1.0 CG2 A:THR334 4.1 15.1 1.0 O A:HOH503 4.1 23.1 1.0 CG A:HIS303 4.2 15.0 1.0 ND1 A:HIS303 4.2 16.6 1.0 CB A:THR334 4.3 13.4 1.0 CB A:ASP240 4.3 11.7 1.0 CG A:GLU367 4.3 13.3 1.0 CG A:GLU336 4.4 16.9 1.0 O A:HOH507 4.4 32.0 0.5 NE2 A:HIS310 4.6 23.9 1.0 O A:HOH555 4.7 28.2 0.5 C1 A:EYF403 4.8 30.8 0.8 CB A:GLU336 4.8 15.6 1.0 OD2 A:ASP229 4.9 19.7 1.0

Cobalt binding site 2 out of 2 in the Crystal Structure of Human Methionine Aminopeptidase (HSMETAP1B) in Complex with An-P2-5H-06


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 An-P2-5H-06 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co402 b:12.8 occ:1.00 OD1 A:ASP240 2.0 12.5 1.0 O1 A:EYF403 2.0 16.6 0.8 OD1 A:ASP229 2.0 17.6 1.0 OE1 A:GLU367 2.1 13.4 1.0 O A:HOH503 2.2 23.1 1.0 N A:EYF403 2.3 35.1 0.8 OD2 A:ASP229 2.4 19.7 1.0 CG A:ASP229 2.5 13.1 1.0 CG A:ASP240 2.9 12.9 1.0 CD A:GLU367 3.0 13.1 1.0 OD2 A:ASP240 3.1 13.3 1.0 CO A:CO401 3.2 16.1 1.0 OE2 A:GLU367 3.3 15.3 1.0 C A:EYF403 3.4 29.1 0.8 O A:EYF403 3.8 24.5 0.8 OG1 A:THR231 3.9 16.3 1.0 ND2 A:ASN242 4.1 12.0 1.0 CB A:ASP229 4.1 12.2 1.0 CB A:ASP240 4.3 11.7 1.0 O A:LEU241 4.3 10.7 1.0 CG A:GLU367 4.4 13.3 1.0 O A:HOH636 4.4 25.2 1.0 N A:LEU241 4.4 10.9 1.0 O A:ILE230 4.4 12.4 1.0 OE2 A:GLU336 4.5 31.2 1.0 O A:HOH532 4.6 21.5 1.0 C A:LEU241 4.6 10.4 1.0 O A:HOH555 4.6 28.2 0.5 C1 A:EYF403 4.6 30.8 0.8 OE1 A:GLU336 4.7 19.5 1.0 C A:ASP240 4.7 11.0 1.0 CA A:ASP240 4.8 11.4 1.0 CA A:ASP229 4.8 10.9 1.0 CB A:ASN242 4.8 10.8 1.0 CB A:GLU367 4.9 11.9 1.0 N A:ILE230 4.9 11.9 1.0 CA A:LEU241 4.9 10.1 1.0 CD A:GLU336 4.9 17.6 1.0 C A:ASP229 5.0 10.6 1.0 CG A:ASN242 5.0 10.9 1.0

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