Copper in PDB 1pu4: Crystal Structure of Human Vascular Adhesion Protein-1

All present enzymatic activity of Crystal Structure of Human Vascular Adhesion Protein-1:
1.4.3.6;

The structure of Crystal Structure of Human Vascular Adhesion Protein-1, PDB code: 1pu4 was solved by T.A.Salminen, T.T.Airenne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 3.20
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	225.916, 225.916, 218.668, 90.00, 90.00, 120.00
R / Rfree (%)	21.7 / 25.4

The structure of Crystal Structure of Human Vascular Adhesion Protein-1 also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Copper atom in the Crystal Structure of Human Vascular Adhesion Protein-1 (pdb code 1pu4). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of Human Vascular Adhesion Protein-1, PDB code: 1pu4:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Crystal Structure of Human Vascular Adhesion Protein-1


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Human Vascular Adhesion Protein-1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu801 b:22.9 occ:1.00 O4 A:TPQ471 2.0 28.8 1.0 ND1 A:HIS684 2.0 25.0 1.0 NE2 A:HIS520 2.0 23.8 1.0 NE2 A:HIS522 2.0 25.3 1.0 CD2 A:HIS522 2.9 26.4 1.0 CE1 A:HIS684 2.9 26.1 1.0 CE1 A:HIS520 3.0 25.0 1.0 C4 A:TPQ471 3.0 30.3 1.0 CD2 A:HIS520 3.0 22.0 1.0 CG A:HIS684 3.1 23.9 1.0 CE1 A:HIS522 3.1 25.6 1.0 CB A:HIS684 3.5 22.7 1.0 C3 A:TPQ471 3.9 32.1 1.0 C5 A:TPQ471 3.9 27.9 1.0 O5 A:TPQ471 3.9 28.0 1.0 NE2 A:HIS684 4.1 24.3 1.0 ND1 A:HIS520 4.1 23.9 1.0 CG A:HIS522 4.1 24.7 1.0 CD2 A:HIS684 4.2 23.5 1.0 CG A:HIS520 4.2 20.6 1.0 ND1 A:HIS522 4.2 26.1 1.0 CE1 A:PHE682 4.9 26.2 1.0

Copper binding site 2 out of 2 in the Crystal Structure of Human Vascular Adhesion Protein-1


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Human Vascular Adhesion Protein-1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu801 b:22.6 occ:1.00 O4 B:TPQ471 2.0 30.8 1.0 ND1 B:HIS684 2.0 24.2 1.0 NE2 B:HIS520 2.0 20.8 1.0 NE2 B:HIS522 2.1 25.0 1.0 CE1 B:HIS684 2.8 26.3 1.0 CE1 B:HIS520 2.9 22.3 1.0 C4 B:TPQ471 2.9 32.3 1.0 CE1 B:HIS522 3.0 26.1 1.0 CG B:HIS684 3.1 22.8 1.0 CD2 B:HIS520 3.1 19.5 1.0 CD2 B:HIS522 3.1 25.8 1.0 CB B:HIS684 3.5 22.4 1.0 C5 B:TPQ471 3.7 29.7 1.0 O5 B:TPQ471 3.8 26.2 1.0 C3 B:TPQ471 3.8 31.9 1.0 NE2 B:HIS684 3.9 24.6 1.0 CD2 B:HIS684 4.1 23.0 1.0 ND1 B:HIS520 4.1 20.1 1.0 ND1 B:HIS522 4.1 25.8 1.0 CG B:HIS522 4.2 23.9 1.0 CG B:HIS520 4.2 18.6 1.0 CE1 B:PHE682 4.8 26.4 1.0 C6 B:TPQ471 4.9 28.7 1.0

T.T.Airenne, Y.Nymalm, H.Kidron, D.J.Smith, M.Pihlavisto, M.Salmi, S.Jalkanen, M.S.Johnson, T.A.Salminen. Crystal Structure of the Human Vascular Adhesion Protein-1: Unique Structural Features with Functional Implications. Protein Sci. V. 14 1964 2005.
ISSN: ISSN 0961-8368
PubMed: 16046623
DOI: 10.1110/PS.051438105