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Zinc in PDB 2fz6: Crystal Structure of Hydrophobin Hfbi

Protein crystallography data

The structure of Crystal Structure of Hydrophobin Hfbi, PDB code: 2fz6 was solved by J.M.Hakanpaa, J.Rouvinen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.10
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 108.900, 49.600, 85.800, 90.00, 129.40, 90.00
R / Rfree (%) 22.4 / 27.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Hydrophobin Hfbi (pdb code 2fz6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Hydrophobin Hfbi, PDB code: 2fz6:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 2fz6

Go back to Zinc Binding Sites List in 2fz6
Zinc binding site 1 out of 4 in the Crystal Structure of Hydrophobin Hfbi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Hydrophobin Hfbi within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:43.5
occ:1.00
OD2 A:ASP30 1.9 35.4 1.0
O A:HOH237 1.9 19.9 1.0
O B:HOH230 2.1 25.7 1.0
OD1 B:ASP30 2.5 35.0 1.0
CG A:ASP30 2.7 50.2 1.0
OD2 B:ASP30 2.8 25.6 1.0
OD1 A:ASP30 2.9 37.8 1.0
CG B:ASP30 3.0 41.9 1.0
O A:HOH206 3.1 40.4 1.0
O B:HOH222 3.7 63.7 1.0
CB A:ASP30 4.2 49.4 1.0
CE A:LYS32 4.3 54.9 1.0
CB B:ASP30 4.5 34.9 1.0
NZ A:LYS32 4.7 59.5 1.0
O A:HOH232 4.8 58.7 1.0
O A:HOH205 4.9 45.6 1.0

Zinc binding site 2 out of 4 in 2fz6

Go back to Zinc Binding Sites List in 2fz6
Zinc binding site 2 out of 4 in the Crystal Structure of Hydrophobin Hfbi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Hydrophobin Hfbi within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn202

b:54.5
occ:1.00
OD2 A:ASP43 1.6 35.8 1.0
OD1 A:ASP40 1.9 27.4 1.0
CG A:ASP43 2.4 38.1 1.0
CG A:ASP40 2.5 38.3 1.0
OD2 A:ASP40 2.6 42.6 1.0
OD1 A:ASP43 2.8 60.5 1.0
N A:ASP43 3.6 32.0 1.0
CB A:ASP43 3.7 33.1 1.0
CB A:THR42 3.8 31.6 1.0
CB A:ASP40 4.0 39.4 1.0
CG2 A:THR42 4.2 22.9 1.0
CA A:ASP43 4.3 30.4 1.0
C A:THR42 4.4 30.2 1.0
N A:ASP40 4.5 38.2 1.0
CA A:THR42 4.5 29.3 1.0
N A:THR42 4.7 42.0 1.0
CA A:ASP40 4.7 43.3 1.0
OG1 A:THR42 4.9 53.7 1.0

Zinc binding site 3 out of 4 in 2fz6

Go back to Zinc Binding Sites List in 2fz6
Zinc binding site 3 out of 4 in the Crystal Structure of Hydrophobin Hfbi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Hydrophobin Hfbi within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn203

b:63.3
occ:1.00
OD1 B:ASP43 2.1 32.7 1.0
OD2 B:ASP43 2.5 59.7 1.0
CG B:ASP43 2.7 23.7 1.0
O B:ASN37 3.4 42.6 1.0
CG2 B:VAL47 3.7 48.5 1.0
O B:HOH205 3.7 38.8 1.0
CB B:ASP43 4.2 28.1 1.0
C B:ASN37 4.5 30.1 1.0
CE2 B:TYR39 4.7 30.7 1.0
CA B:VAL38 4.9 36.7 1.0
CA B:ASP43 4.9 41.1 1.0
N B:VAL38 4.9 30.5 1.0
CD2 B:TYR39 5.0 8.7 1.0

Zinc binding site 4 out of 4 in 2fz6

Go back to Zinc Binding Sites List in 2fz6
Zinc binding site 4 out of 4 in the Crystal Structure of Hydrophobin Hfbi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Hydrophobin Hfbi within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn204

b:58.8
occ:1.00
OD1 D:ASP30 2.0 52.6 1.0
OD2 C:ASP30 2.3 32.4 1.0
CG D:ASP30 3.2 54.9 1.0
CG C:ASP30 3.2 11.4 1.0
OD1 C:ASP30 3.4 32.9 1.0
OD2 D:ASP30 3.8 50.7 1.0
O D:HOH77 4.0 22.5 1.0
NZ C:LYS32 4.1 49.4 1.0
CB D:ASP30 4.3 60.3 1.0
CA D:ASP30 4.5 55.5 1.0
CB C:ASP30 4.6 9.2 1.0
N D:ASP30 4.8 44.6 1.0
CE C:LYS32 4.8 55.6 1.0
O C:HOH211 4.9 37.6 1.0

Reference:

J.M.Hakanpaa, G.R.Szilvay, H.Kaljunen, M.Maksimainen, M.Linder, J.Rouvinen. Two Crystal Structures of Trichoderma Reesei Hydrophobin Hfbi--the Structure of A Protein Amphiphile with and Without Detergent Interaction. Protein Sci. V. 15 2129 2006.
ISSN: ISSN 0961-8368
PubMed: 16882996
DOI: 10.1110/PS.062326706
Page generated: Wed Dec 16 03:28:46 2020

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