Atomistry » Zinc » PDB 3l2q-3liz » 3li2
Atomistry »
  Zinc »
    PDB 3l2q-3liz »
      3li2 »

Zinc in PDB 3li2: Closed Conformation of Htsa Complexed with Staphyloferrin A

Protein crystallography data

The structure of Closed Conformation of Htsa Complexed with Staphyloferrin A, PDB code: 3li2 was solved by J.C.Grigg, M.E.P.Murphy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.15 / 2.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 52.280, 148.600, 52.270, 90.00, 117.14, 90.00
R / Rfree (%) 16.5 / 21.6

Other elements in 3li2:

The structure of Closed Conformation of Htsa Complexed with Staphyloferrin A also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Closed Conformation of Htsa Complexed with Staphyloferrin A (pdb code 3li2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Closed Conformation of Htsa Complexed with Staphyloferrin A, PDB code: 3li2:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 3li2

Go back to Zinc Binding Sites List in 3li2
Zinc binding site 1 out of 4 in the Closed Conformation of Htsa Complexed with Staphyloferrin A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Closed Conformation of Htsa Complexed with Staphyloferrin A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1

b:33.8
occ:1.00
NE2 A:HIS266 1.8 29.0 1.0
O A:HOH404 2.2 34.0 1.0
CE1 A:HIS266 2.6 30.6 1.0
CD2 A:HIS266 2.9 28.2 1.0
O A:HOH363 3.0 47.2 1.0
ND1 A:HIS266 3.8 30.3 1.0
CG A:HIS266 4.0 28.1 1.0
OG A:SER271 4.1 49.0 1.0
O A:HOH331 4.6 23.2 1.0
O A:HOH414 4.6 36.5 1.0
CB A:SER271 4.7 46.9 1.0
CA A:SER271 5.0 47.8 1.0

Zinc binding site 2 out of 4 in 3li2

Go back to Zinc Binding Sites List in 3li2
Zinc binding site 2 out of 4 in the Closed Conformation of Htsa Complexed with Staphyloferrin A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Closed Conformation of Htsa Complexed with Staphyloferrin A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2

b:26.1
occ:1.00
OD1 A:ASP270 1.7 38.6 1.0
ND1 A:HIS266 2.4 30.3 1.0
CG A:ASP270 2.6 46.2 1.0
OD2 A:ASP270 2.8 45.9 1.0
CG A:HIS266 3.0 28.1 1.0
CB A:HIS266 3.2 28.0 1.0
CE1 A:HIS266 3.4 30.6 1.0
N A:SER271 3.9 47.1 1.0
CB A:ASP270 4.1 48.7 1.0
CD2 A:HIS266 4.2 28.2 1.0
CA A:HIS266 4.3 27.8 1.0
NE2 A:HIS266 4.4 29.0 1.0
N A:ASP270 4.5 46.1 1.0
CA A:ASP270 4.6 47.0 1.0
CB A:LYS268 4.6 47.9 1.0
CA A:SER271 4.6 47.8 1.0
C A:ASP270 4.8 46.8 1.0
N A:LYS268 4.9 45.6 1.0
C A:HIS266 4.9 28.1 1.0

Zinc binding site 3 out of 4 in 3li2

Go back to Zinc Binding Sites List in 3li2
Zinc binding site 3 out of 4 in the Closed Conformation of Htsa Complexed with Staphyloferrin A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Closed Conformation of Htsa Complexed with Staphyloferrin A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn3

b:24.0
occ:1.00
OD1 A:ASP248 1.8 23.5 1.0
ND1 A:HIS251 2.1 30.8 1.0
OD2 A:ASP248 2.4 31.3 1.0
CG A:ASP248 2.4 28.7 1.0
CG A:HIS251 3.0 29.1 1.0
CE1 A:HIS251 3.1 32.2 1.0
CB A:HIS251 3.3 27.1 1.0
N A:HIS251 3.4 28.3 1.0
CA A:HIS251 3.6 28.0 1.0
O A:HOH416 3.6 25.3 1.0
CB A:ASP248 3.9 29.5 1.0
CD2 A:HIS251 4.1 27.8 1.0
NE2 A:HIS251 4.2 31.6 1.0
C A:GLU250 4.3 30.1 1.0
N A:ASP248 4.7 28.2 1.0
CA A:ASP248 4.8 29.0 1.0
CB A:GLU250 4.9 33.1 1.0

Zinc binding site 4 out of 4 in 3li2

Go back to Zinc Binding Sites List in 3li2
Zinc binding site 4 out of 4 in the Closed Conformation of Htsa Complexed with Staphyloferrin A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Closed Conformation of Htsa Complexed with Staphyloferrin A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn4

b:34.8
occ:1.00
OD2 A:ASP254 2.2 34.6 1.0
OD1 A:ASP254 2.3 34.7 1.0
CG A:ASP254 2.6 34.7 1.0
O A:HOH373 3.4 34.0 1.0
CB A:ASP254 4.1 33.3 1.0
O A:GLU250 4.2 30.5 1.0
OE1 A:GLU250 4.5 41.8 1.0
C A:GLU250 4.9 30.1 1.0

Reference:

J.C.Grigg, J.D.Cooper, J.Cheung, D.E.Heinrichs, M.E.Murphy. The Staphylococcus Aureus Siderophore Receptor Htsa Undergoes Localized Conformational Changes to Enclose Staphyloferrin A in An Arginine-Rich Binding Pocket. J.Biol.Chem. V. 285 11162 2010.
ISSN: ISSN 0021-9258
PubMed: 20147287
DOI: 10.1074/JBC.M109.097865
Page generated: Wed Dec 16 04:32:19 2020

Last articles

Zn in 7RRP
Zn in 7OKY
Zn in 7OL0
Zn in 7OKX
Zn in 7ONB
Zn in 7RSF
Zn in 7OUF
Zn in 7OUG
Zn in 7OUH
Zn in 7RGN
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy