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Zinc in PDB 2qt3: Crystal Structure of N-Isopropylammelide Isopropylaminohydrolase Atzc From Pseudomonas Sp. Strain Adp Complexed with Zn

Enzymatic activity of Crystal Structure of N-Isopropylammelide Isopropylaminohydrolase Atzc From Pseudomonas Sp. Strain Adp Complexed with Zn

All present enzymatic activity of Crystal Structure of N-Isopropylammelide Isopropylaminohydrolase Atzc From Pseudomonas Sp. Strain Adp Complexed with Zn:
3.5.99.4;

Protein crystallography data

The structure of Crystal Structure of N-Isopropylammelide Isopropylaminohydrolase Atzc From Pseudomonas Sp. Strain Adp Complexed with Zn, PDB code: 2qt3 was solved by A.A.Fedorov, E.V.Fedorov, J.Seffernick, L.P.Wackett, S.K.Burley, S.C.Almo, New York Sgx Research Center For Structural Genomics (Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.97 / 2.24
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 102.969, 102.969, 225.558, 90.00, 90.00, 90.00
R / Rfree (%) 22.6 / 24.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of N-Isopropylammelide Isopropylaminohydrolase Atzc From Pseudomonas Sp. Strain Adp Complexed with Zn (pdb code 2qt3). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of N-Isopropylammelide Isopropylaminohydrolase Atzc From Pseudomonas Sp. Strain Adp Complexed with Zn, PDB code: 2qt3:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2qt3

Go back to Zinc Binding Sites List in 2qt3
Zinc binding site 1 out of 2 in the Crystal Structure of N-Isopropylammelide Isopropylaminohydrolase Atzc From Pseudomonas Sp. Strain Adp Complexed with Zn


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 N-Isopropylammelide Isopropylaminohydrolase Atzc From Pseudomonas Sp. Strain Adp Complexed with Zn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:31.9
occ:1.00
NE2 A:HIS62 2.1 22.0 1.0
NE2 A:HIS60 2.1 20.8 1.0
O A:HOH594 2.1 36.6 1.0
NE2 A:HIS217 2.3 22.7 1.0
OD1 A:ASP303 2.7 25.4 1.0
CE1 A:HIS62 3.0 21.4 1.0
CE1 A:HIS60 3.1 24.1 1.0
CD2 A:HIS60 3.1 21.6 1.0
CD2 A:HIS62 3.1 23.0 1.0
CD2 A:HIS217 3.2 24.3 1.0
CE1 A:HIS217 3.3 26.0 1.0
CG A:ASP303 3.7 28.7 1.0
NE2 A:HIS249 3.9 35.6 1.0
OD2 A:ASP303 4.0 26.9 1.0
ND1 A:HIS62 4.1 22.2 1.0
ND1 A:HIS60 4.2 22.4 1.0
CG A:HIS62 4.2 23.3 1.0
CG A:HIS60 4.2 21.3 1.0
CG A:HIS217 4.4 24.2 1.0
ND1 A:HIS217 4.4 23.8 1.0
ND2 A:ASN304 4.5 14.5 1.0
CE1 A:HIS249 4.6 33.7 1.0
CD2 A:HIS249 4.9 33.7 1.0
ND1 A:HIS125 4.9 27.8 1.0

Zinc binding site 2 out of 2 in 2qt3

Go back to Zinc Binding Sites List in 2qt3
Zinc binding site 2 out of 2 in the Crystal Structure of N-Isopropylammelide Isopropylaminohydrolase Atzc From Pseudomonas Sp. Strain Adp Complexed with Zn


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 N-Isopropylammelide Isopropylaminohydrolase Atzc From Pseudomonas Sp. Strain Adp Complexed with Zn within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn502

b:44.2
occ:1.00
NE2 B:HIS62 2.1 37.3 1.0
NE2 B:HIS60 2.1 28.9 1.0
O B:HOH567 2.4 65.3 1.0
NE2 B:HIS217 2.4 39.3 1.0
OD1 B:ASP303 2.7 41.9 1.0
CE1 B:HIS62 3.1 33.4 1.0
CE1 B:HIS60 3.1 31.0 1.0
CD2 B:HIS60 3.1 30.8 1.0
CD2 B:HIS62 3.1 33.9 1.0
CD2 B:HIS217 3.2 38.1 1.0
CE1 B:HIS217 3.4 39.1 1.0
CG B:ASP303 3.7 39.4 1.0
NE2 B:HIS249 3.8 40.8 1.0
OD2 B:ASP303 3.9 43.6 1.0
ND1 B:HIS62 4.2 35.4 1.0
ND1 B:HIS60 4.2 32.8 1.0
CG B:HIS62 4.3 35.6 1.0
CG B:HIS60 4.3 30.6 1.0
CG B:HIS217 4.4 38.8 1.0
ND2 B:ASN304 4.4 33.3 1.0
ND1 B:HIS217 4.4 38.0 1.0
CE1 B:HIS249 4.5 39.1 1.0
CD2 B:HIS249 4.8 37.0 1.0

Reference:

A.A.Fedorov, E.V.Fedorov, J.Seffernick, L.P.Wackett, S.K.Burley, S.C.Almo. Crystal Structure of N-Isopropylammelide Isopropylaminohydrolase Atzc From Pseudomonas Sp. Strain Adp Complexed with Zn. To Be Published.
Page generated: Thu Oct 17 03:36:07 2024

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