Atomistry » Copper » PDB 1oe2-1rjp » 1us1
Atomistry »
  Copper »
    PDB 1oe2-1rjp »
      1us1 »

Copper in PDB 1us1: Crystal Structure of Human Vascular Adhesion Protein-1

Enzymatic activity of 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;

Protein crystallography data

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

Copper Binding Sites:

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 1us1

Go back to Copper Binding Sites List in 1us1
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 1us1

Go back to Copper Binding Sites List in 1us1
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

Reference:

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
Page generated: Thu Sep 3 16:21:39 2020
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy