Cobalt in PDB 2erp: Crystal Structure of Vascular Apoptosis-Inducing Protein-1(Inhibitor- Bound Form)

The structure of Crystal Structure of Vascular Apoptosis-Inducing Protein-1(Inhibitor- Bound Form), PDB code: 2erp was solved by S.Takeda, T.Igarashi, S.Araki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	86.345, 91.379, 136.039, 90.00, 90.00, 90.00
R / Rfree (%)	20.8 / 26.4

The structure of Crystal Structure of Vascular Apoptosis-Inducing Protein-1(Inhibitor- Bound Form) also contains other interesting chemical elements:

Calcium	(Ca)	4 atoms
Zinc	(Zn)	2 atoms

The binding sites of Cobalt atom in the Crystal Structure of Vascular Apoptosis-Inducing Protein-1(Inhibitor- Bound Form) (pdb code 2erp). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Crystal Structure of Vascular Apoptosis-Inducing Protein-1(Inhibitor- Bound Form), PDB code: 2erp:

Cobalt binding site 1 out of 1 in the Crystal Structure of Vascular Apoptosis-Inducing Protein-1(Inhibitor- Bound Form)


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 Vascular Apoptosis-Inducing Protein-1(Inhibitor- Bound Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Co703 b:56.8 occ:1.00 NE2 A:HIS243 2.2 46.8 1.0 NE2 A:HIS238 2.6 38.7 1.0 CE1 A:HIS243 3.1 41.4 1.0 CD2 A:HIS243 3.4 48.3 1.0 CE1 A:HIS238 3.5 45.0 1.0 CD2 A:HIS238 3.5 42.2 1.0 NZ A:LYS198 4.0 56.0 1.0 ND1 A:HIS243 4.2 39.1 1.0 CG A:HIS243 4.4 49.3 1.0 OE1 A:GLU445 4.5 76.5 1.0 ND1 A:HIS238 4.6 42.7 1.0 CD A:LYS198 4.6 61.6 1.0 CG A:HIS238 4.6 44.5 1.0 CE A:LYS198 4.6 60.8 1.0 O A:TYR409 4.7 47.3 1.0 CB A:TYR409 5.0 36.0 1.0

S.Takeda, T.Igarashi, H.Mori, S.Araki. Crystal Structures of VAP1 Reveal Adams' Mdc Domain Architecture and Its Unique C-Shaped Scaffold Embo J. V. 25 2388 2006.
ISSN: ISSN 0261-4189
PubMed: 16688218
DOI: 10.1038/SJ.EMBOJ.7601131