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Zinc in PDB 5cgz: Crystal Structure of Galb, the 4-Carboxy-2-Hydroxymuconate Hydratase, From Pseuodomonas Putida KT2440

Enzymatic activity of Crystal Structure of Galb, the 4-Carboxy-2-Hydroxymuconate Hydratase, From Pseuodomonas Putida KT2440

All present enzymatic activity of Crystal Structure of Galb, the 4-Carboxy-2-Hydroxymuconate Hydratase, From Pseuodomonas Putida KT2440:
4.2.1.83;

Protein crystallography data

The structure of Crystal Structure of Galb, the 4-Carboxy-2-Hydroxymuconate Hydratase, From Pseuodomonas Putida KT2440, PDB code: 5cgz was solved by S.Mazurkewich, A.S.Brott, M.S.Kimber, S.Y.K.Seah, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.91 / 2.10
Space group P 41 3 2
Cell size a, b, c (Å), α, β, γ (°) 201.660, 201.660, 201.660, 90.00, 90.00, 90.00
R / Rfree (%) 15 / 17

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Galb, the 4-Carboxy-2-Hydroxymuconate Hydratase, From Pseuodomonas Putida KT2440 (pdb code 5cgz). 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 Galb, the 4-Carboxy-2-Hydroxymuconate Hydratase, From Pseuodomonas Putida KT2440, PDB code: 5cgz:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 5cgz

Go back to Zinc Binding Sites List in 5cgz
Zinc binding site 1 out of 2 in the Crystal Structure of Galb, the 4-Carboxy-2-Hydroxymuconate Hydratase, From Pseuodomonas Putida KT2440


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 Galb, the 4-Carboxy-2-Hydroxymuconate Hydratase, From Pseuodomonas Putida KT2440 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:35.0
occ:1.00
OE2 A:GLU48 2.0 34.3 0.6
OD1 A:ASP17 2.0 34.1 1.0
ND1 A:HIS14 2.1 31.8 1.0
NE2 A:HIS127 2.2 34.2 1.0
O A:HOH401 2.5 47.8 1.0
CG A:ASP17 2.8 35.4 1.0
CD A:GLU48 2.9 40.6 0.6
OD2 A:ASP17 2.9 43.0 1.0
CE1 A:HIS14 3.0 33.0 1.0
CD2 A:HIS127 3.1 32.4 1.0
OE1 A:GLU48 3.1 47.0 0.6
CG A:HIS14 3.1 37.6 1.0
CE1 A:HIS127 3.2 34.6 1.0
CB A:HIS14 3.5 28.9 1.0
OE2 A:GLU48 3.7 44.0 0.4
NE2 A:HIS14 4.1 32.5 1.0
ND2 A:ASN124 4.2 42.3 1.0
CD2 A:HIS14 4.2 30.8 1.0
CB A:ASP17 4.2 30.3 1.0
CG A:GLU48 4.3 36.6 0.6
ND1 A:HIS127 4.3 32.0 1.0
CG A:HIS127 4.3 31.2 1.0
N A:HIS14 4.3 32.1 1.0
CD A:GLU48 4.3 35.5 0.4
CE1 A:HIS117 4.4 29.1 1.0
CG A:GLU48 4.4 42.3 0.4
CA A:HIS14 4.5 35.6 1.0
CB A:ALA13 4.8 30.0 1.0
CG A:ASN124 4.9 44.4 1.0
O A:HOH432 5.0 61.2 1.0

Zinc binding site 2 out of 2 in 5cgz

Go back to Zinc Binding Sites List in 5cgz
Zinc binding site 2 out of 2 in the Crystal Structure of Galb, the 4-Carboxy-2-Hydroxymuconate Hydratase, From Pseuodomonas Putida KT2440


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 Galb, the 4-Carboxy-2-Hydroxymuconate Hydratase, From Pseuodomonas Putida KT2440 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn301

b:34.9
occ:1.00
OD2 B:ASP17 2.0 32.9 1.0
ND1 B:HIS14 2.0 31.1 1.0
OE2 B:GLU48 2.1 31.0 0.6
NE2 B:HIS127 2.1 35.3 1.0
CG B:ASP17 2.8 34.3 1.0
CD B:GLU48 2.8 40.0 0.6
CE1 B:HIS14 2.9 32.3 1.0
O B:HOH403 3.0 55.6 1.0
OD1 B:ASP17 3.0 36.8 1.0
OE1 B:GLU48 3.0 39.8 0.6
CD2 B:HIS127 3.1 30.5 1.0
CE1 B:HIS127 3.1 32.8 1.0
CG B:HIS14 3.1 32.7 1.0
CB B:HIS14 3.5 31.4 1.0
OE2 B:GLU48 3.9 37.0 0.4
NE2 B:HIS14 4.1 32.6 1.0
ND2 B:ASN124 4.2 43.6 1.0
CD B:GLU48 4.2 34.4 0.4
CD2 B:HIS14 4.2 30.7 1.0
CB B:ASP17 4.2 26.0 1.0
ND1 B:HIS127 4.2 32.2 1.0
CG B:GLU48 4.2 35.0 0.6
CG B:HIS127 4.2 33.3 1.0
N B:HIS14 4.2 30.5 1.0
CG B:GLU48 4.4 34.6 0.4
CE1 B:HIS117 4.4 31.4 1.0
CA B:HIS14 4.5 32.4 1.0
CB B:ALA13 4.7 30.8 1.0
OE1 B:GLU48 4.9 32.0 0.4
CG B:ASN124 4.9 44.7 1.0

Reference:

S.Mazurkewich, A.S.Brott, M.S.Kimber, S.Y.Seah. Structural and Kinetic Characterization of the 4-Carboxy-2-Hydroxymuconate Hydratase From the Gallate and Protocatechuate 4,5-Cleavage Pathways of Pseudomonas Putida KT2440. J.Biol.Chem. V. 291 7669 2016.
ISSN: ESSN 1083-351X
PubMed: 26867578
DOI: 10.1074/JBC.M115.682054
Page generated: Thu Aug 21 01:25:57 2025

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