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Zinc in PDB 3o2g: Crystal Structure of Human Gamma-Butyrobetaine,2-Oxoglutarate Dioxygenase 1 (BBOX1)

Enzymatic activity of Crystal Structure of Human Gamma-Butyrobetaine,2-Oxoglutarate Dioxygenase 1 (BBOX1)

All present enzymatic activity of Crystal Structure of Human Gamma-Butyrobetaine,2-Oxoglutarate Dioxygenase 1 (BBOX1):
1.14.11.1;

Protein crystallography data

The structure of Crystal Structure of Human Gamma-Butyrobetaine,2-Oxoglutarate Dioxygenase 1 (BBOX1), PDB code: 3o2g was solved by T.Krojer, G.Kochan, M.A.Mcdonough, F.Von Delft, I.K.H.Leung, L.Henry, T.D.W.Claridge, E.Pilka, E.Ugochukwu, J.Muniz, P.Filippakopoulos, C.Bountra, C.H.Arrowsmith, J.Weigelt, A.Edwards, K.L.Kavanagh, C.J.Schofield, U.Oppermann, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.98 / 1.78
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 107.386, 107.386, 204.919, 90.00, 90.00, 120.00
R / Rfree (%) 14.7 / 17.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human Gamma-Butyrobetaine,2-Oxoglutarate Dioxygenase 1 (BBOX1) (pdb code 3o2g). 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 Human Gamma-Butyrobetaine,2-Oxoglutarate Dioxygenase 1 (BBOX1), PDB code: 3o2g:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3o2g

Go back to Zinc Binding Sites List in 3o2g
Zinc binding site 1 out of 2 in the Crystal Structure of Human Gamma-Butyrobetaine,2-Oxoglutarate Dioxygenase 1 (BBOX1)


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 Gamma-Butyrobetaine,2-Oxoglutarate Dioxygenase 1 (BBOX1) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn388

b:14.1
occ:1.00
O A:HOH744 2.1 17.1 1.0
NE2 A:HIS202 2.1 11.7 1.0
O2 A:OGA390 2.1 16.4 1.0
NE2 A:HIS347 2.1 12.2 1.0
O2' A:OGA390 2.1 13.5 1.0
OD1 A:ASP204 2.1 11.6 1.0
C1 A:OGA390 2.8 17.3 1.0
C2 A:OGA390 2.8 16.7 1.0
CE1 A:HIS202 3.0 12.9 1.0
CD2 A:HIS347 3.0 12.2 1.0
CG A:ASP204 3.1 12.1 1.0
CD2 A:HIS202 3.1 12.3 1.0
CE1 A:HIS347 3.1 12.4 1.0
OD2 A:ASP204 3.4 13.7 1.0
O1 A:OGA390 4.0 19.0 1.0
N1 A:OGA390 4.1 16.4 1.0
ND1 A:HIS202 4.1 12.9 1.0
ND1 A:HIS347 4.2 11.8 1.0
CG A:HIS347 4.2 11.4 1.0
O A:HOH553 4.2 22.9 1.0
CG A:HIS202 4.2 11.2 1.0
OE1 A:GLN215 4.3 17.7 1.0
NE2 A:GLN215 4.3 15.4 1.0
CB A:ASP204 4.4 11.8 1.0
CD A:GLN215 4.7 17.1 1.0
C4 A:OGA390 4.8 15.5 1.0
C3 A:NM2391 4.8 14.2 1.0
C6 A:NM2391 4.8 14.8 1.0
CA A:ASP204 4.8 11.2 1.0
CD1 A:LEU199 5.0 14.5 1.0
N A:ASP204 5.0 11.6 1.0

Zinc binding site 2 out of 2 in 3o2g

Go back to Zinc Binding Sites List in 3o2g
Zinc binding site 2 out of 2 in the Crystal Structure of Human Gamma-Butyrobetaine,2-Oxoglutarate Dioxygenase 1 (BBOX1)


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 Gamma-Butyrobetaine,2-Oxoglutarate Dioxygenase 1 (BBOX1) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn389

b:14.1
occ:1.00
NE2 A:HIS82 2.1 13.7 1.0
SG A:CYS38 2.3 13.9 1.0
SG A:CYS40 2.3 14.8 1.0
SG A:CYS43 2.3 12.5 1.0
CE1 A:HIS82 3.0 15.2 1.0
CD2 A:HIS82 3.2 13.3 1.0
CB A:CYS38 3.3 12.1 1.0
CB A:CYS43 3.3 13.2 1.0
CB A:CYS40 3.4 15.3 1.0
O A:HOH767 4.0 32.9 1.0
N A:CYS40 4.1 14.5 1.0
NH1 A:ARG35 4.1 12.0 1.0
N A:CYS43 4.2 13.1 1.0
ND1 A:HIS82 4.2 15.6 1.0
CA A:CYS40 4.2 14.5 1.0
CG A:HIS82 4.3 14.0 1.0
CA A:CYS43 4.4 12.9 1.0
O A:TYR83 4.4 15.4 1.0
CA A:CYS38 4.5 11.9 1.0
C A:CYS38 4.5 11.9 1.0
O A:CYS38 4.6 12.0 1.0
OG A:SER84 4.6 12.5 1.0
O A:CYS40 4.6 13.9 1.0
O A:HOH583 4.6 22.5 1.0
C A:CYS40 4.7 14.4 1.0
CZ A:ARG35 4.7 12.4 1.0
NH2 A:ARG35 4.7 12.2 1.0
CB A:ASP42 4.8 15.6 1.0

Reference:

I.K.Leung, T.J.Krojer, G.T.Kochan, L.Henry, F.Von Delft, T.D.Claridge, U.Oppermann, M.A.Mcdonough, C.J.Schofield. Structural and Mechanistic Studies on Gamma-Butyrobetaine Hydroxylase. Chem. Biol. V. 17 1316 2010.
ISSN: ISSN 1879-1301
PubMed: 21168767
DOI: 10.1016/J.CHEMBIOL.2010.09.016
Page generated: Sat Oct 26 10:40:30 2024

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