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Zinc in PDB 2xsn: Crystal Structure of Human Tyrosine Hydroxylase Catalytic Domain

Enzymatic activity of Crystal Structure of Human Tyrosine Hydroxylase Catalytic Domain

All present enzymatic activity of Crystal Structure of Human Tyrosine Hydroxylase Catalytic Domain:
1.14.16.2;

Protein crystallography data

The structure of Crystal Structure of Human Tyrosine Hydroxylase Catalytic Domain, PDB code: 2xsn was solved by J.R.C.Muniz, C.D.O.Cooper, W.W.Yue, E.Krysztofinska, F.Von Delft, S.Knapp, O.Gileadi, C.H.Arrowsmith, A.M.Edwards, J.Weigelt, C.Bountra, K.L.Kavanagh, U.Oppermann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 62.66 / 2.68
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 191.420, 191.420, 168.160, 90.00, 90.00, 120.00
R / Rfree (%) 18.9 / 22.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human Tyrosine Hydroxylase Catalytic Domain (pdb code 2xsn). 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 Human Tyrosine Hydroxylase Catalytic Domain, PDB code: 2xsn:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 2xsn

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Zinc binding site 1 out of 4 in the Crystal Structure of Human Tyrosine Hydroxylase Catalytic Domain


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 Human Tyrosine Hydroxylase Catalytic Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1528

b:60.1
occ:1.00
NE2 A:HIS366 2.1 48.3 1.0
OE2 A:GLU406 2.2 62.5 1.0
NE2 A:HIS361 2.2 49.1 1.0
OE1 A:GLU406 2.8 42.9 1.0
O A:HOH2067 2.8 52.9 1.0
CD A:GLU406 2.8 61.4 1.0
CD2 A:HIS366 3.1 48.7 1.0
CE1 A:HIS366 3.1 47.1 1.0
CE1 A:HIS361 3.2 50.2 1.0
CD2 A:HIS361 3.3 49.4 1.0
CG A:HIS366 4.2 46.1 1.0
CG A:GLU406 4.2 44.6 1.0
ND1 A:HIS366 4.3 47.4 1.0
ND1 A:HIS361 4.3 51.2 1.0
CG A:HIS361 4.4 47.8 1.0
CB A:ALA421 4.5 44.0 1.0
OE1 A:GLU362 4.7 47.5 1.0
O A:HOH2033 4.8 42.9 1.0

Zinc binding site 2 out of 4 in 2xsn

Go back to Zinc Binding Sites List in 2xsn
Zinc binding site 2 out of 4 in the Crystal Structure of Human Tyrosine Hydroxylase Catalytic Domain


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 Human Tyrosine Hydroxylase Catalytic Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1529

b:57.8
occ:1.00
NE2 B:HIS361 2.2 47.6 1.0
OE2 B:GLU406 2.2 64.1 1.0
NE2 B:HIS366 2.3 44.0 1.0
O B:HOH2068 2.5 52.4 1.0
CD B:GLU406 2.9 69.9 1.0
OE1 B:GLU406 2.9 58.6 1.0
CE1 B:HIS361 3.2 48.8 1.0
CD2 B:HIS361 3.3 46.6 1.0
O B:HOH2067 3.3 47.0 1.0
CD2 B:HIS366 3.3 43.5 1.0
CE1 B:HIS366 3.3 43.6 1.0
O B:HOH2045 3.9 53.9 1.0
CG B:GLU406 4.3 55.0 1.0
ND1 B:HIS361 4.3 49.0 1.0
CG B:HIS361 4.4 45.2 1.0
CG B:HIS366 4.4 41.5 1.0
ND1 B:HIS366 4.4 43.7 1.0
CB B:ALA421 4.6 38.5 1.0
OE1 B:GLU362 4.7 51.1 1.0
CB B:PRO357 5.0 50.8 1.0

Zinc binding site 3 out of 4 in 2xsn

Go back to Zinc Binding Sites List in 2xsn
Zinc binding site 3 out of 4 in the Crystal Structure of Human Tyrosine Hydroxylase Catalytic Domain


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 Human Tyrosine Hydroxylase Catalytic Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn1536

b:77.8
occ:1.00
OE2 C:GLU406 2.2 79.7 1.0
NE2 C:HIS361 2.2 51.0 1.0
NE2 C:HIS366 2.3 50.9 1.0
CD C:GLU406 2.8 85.5 1.0
OE1 C:GLU406 2.8 85.0 1.0
CE1 C:HIS361 3.1 50.9 1.0
CD2 C:HIS366 3.2 49.9 1.0
CD2 C:HIS361 3.3 51.0 1.0
CE1 C:HIS366 3.3 50.7 1.0
CG C:GLU406 4.3 64.0 1.0
ND1 C:HIS361 4.3 51.2 1.0
CG C:HIS361 4.4 48.9 1.0
CG C:HIS366 4.4 46.7 1.0
ND1 C:HIS366 4.4 49.8 1.0
CB C:ALA421 4.5 43.1 1.0
OE1 C:GLU362 4.5 48.2 1.0
O C:HOH2039 4.7 48.9 1.0
CB C:PRO357 4.8 57.2 1.0

Zinc binding site 4 out of 4 in 2xsn

Go back to Zinc Binding Sites List in 2xsn
Zinc binding site 4 out of 4 in the Crystal Structure of Human Tyrosine Hydroxylase Catalytic Domain


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 Human Tyrosine Hydroxylase Catalytic Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn1536

b:84.0
occ:1.00
NE2 D:HIS366 2.3 56.0 1.0
NE2 D:HIS361 2.5 49.5 1.0
OE1 D:GLU406 2.7 92.2 1.0
OE2 D:GLU406 2.8 79.2 1.0
CE1 D:HIS366 3.0 55.9 1.0
CD D:GLU406 3.1 84.4 1.0
CD2 D:HIS361 3.3 48.6 1.0
CD2 D:HIS366 3.4 55.4 1.0
CE1 D:HIS361 3.6 50.9 1.0
ND1 D:HIS366 4.3 55.8 1.0
OE1 D:GLU362 4.4 52.4 1.0
CG D:HIS366 4.4 53.4 1.0
CG D:HIS361 4.5 47.4 1.0
CG D:GLU406 4.5 69.5 1.0
ND1 D:HIS361 4.6 51.2 1.0
CB D:PRO357 4.7 44.1 1.0
CB D:ALA421 4.7 64.9 1.0
OH D:TYR401 4.8 79.0 1.0

Reference:

J.R.C.Muniz, C.D.O.Cooper, W.W.Yue, E.Krysztofinska, F.Von Delft, S.Knapp, O.Gileadi, C.H.Arrowsmith, A.M.Edwards, J.Weigelt, C.Bountra, K.L.Kavanagh, U.Oppermann. Crystal Structure of Human Tyrosine Hydroxylase Catalytic Domain To Be Published.
Page generated: Thu Oct 17 05:31:43 2024

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