Copper in PDB 1us1: 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: 1us1 was solved by T.T.Airenne, Y.Nymalm, H.Kidron, A.Soderholm, M.S.Johnson, T.A.Salminen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.96 / 2.90
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	226.099, 226.099, 223.004, 90.00, 90.00, 120.00
R / Rfree (%)	24.1 / 26.7

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 1us1). 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: 1us1:
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:Cu1762 b:36.0 occ:1.00 O4 A:TPQ471 2.0 42.5 1.0 ND1 A:HIS684 2.0 34.6 1.0 NE2 A:HIS522 2.0 38.5 1.0 NE2 A:HIS520 2.1 33.4 1.0 CE1 A:HIS684 2.8 35.0 1.0 CE1 A:HIS520 3.0 34.2 1.0 C4 A:TPQ471 3.0 43.3 1.0 CE1 A:HIS522 3.0 38.5 1.0 CD2 A:HIS522 3.1 37.7 1.0 CD2 A:HIS520 3.1 33.3 1.0 CG A:HIS684 3.1 34.0 1.0 CB A:HIS684 3.6 34.5 1.0 O5 A:TPQ471 3.8 37.7 1.0 C5 A:TPQ471 3.8 40.4 1.0 C3 A:TPQ471 3.9 43.5 1.0 NE2 A:HIS684 4.0 33.8 1.0 ND1 A:HIS522 4.1 38.9 1.0 ND1 A:HIS520 4.1 33.4 1.0 CD2 A:HIS684 4.2 32.5 1.0 CG A:HIS522 4.2 36.5 1.0 CG A:HIS520 4.2 33.6 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:Cu1762 b:38.5 occ:1.00 O4 B:TPQ471 2.0 42.6 1.0 ND1 B:HIS684 2.0 37.1 1.0 NE2 B:HIS520 2.0 30.6 1.0 NE2 B:HIS522 2.1 39.9 1.0 CE1 B:HIS684 2.9 38.1 1.0 C4 B:TPQ471 3.0 41.9 1.0 CE1 B:HIS520 3.0 31.1 1.0 CG B:HIS684 3.1 33.7 1.0 CE1 B:HIS522 3.1 39.8 1.0 CD2 B:HIS522 3.1 38.6 1.0 CD2 B:HIS520 3.1 29.3 1.0 CB B:HIS684 3.5 33.3 1.0 C5 B:TPQ471 3.7 40.3 1.0 O5 B:TPQ471 3.8 34.6 1.0 C3 B:TPQ471 3.9 42.6 1.0 NE2 B:HIS684 4.0 35.8 1.0 CD2 B:HIS684 4.1 33.6 1.0 ND1 B:HIS520 4.1 30.5 1.0 ND1 B:HIS522 4.2 39.5 1.0 CG B:HIS520 4.2 29.7 1.0 CG B:HIS522 4.2 36.8 1.0 CE1 B:PHE682 4.8 38.6 1.0 C6 B:TPQ471 5.0 42.2 1.0 CA B:HIS684 5.0 33.9 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