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Magnesium in PDB 3vcn: Crystal Structure of Mannonate Dehydratase (Target Efi-502209) From Caulobacter Crescentus CB15

Protein crystallography data

The structure of Crystal Structure of Mannonate Dehydratase (Target Efi-502209) From Caulobacter Crescentus CB15, PDB code: 3vcn was solved by Y.Patskovsky, R.Toro, R.Bhosle, B.Hillerich, R.D.Seidel, E.Washington, A.Scott Glenn, S.Chowdhury, B.Evans, J.Hammonds, W.D.Zencheck, H.J.Imker, J.A.Gerlt, S.C.Almo, Enzyme Function Initiative (Efi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.45
Space group I 4
Cell size a, b, c (Å), α, β, γ (°) 116.302, 116.302, 118.078, 90.00, 90.00, 90.00
R / Rfree (%) 13 / 18.8

Other elements in 3vcn:

The structure of Crystal Structure of Mannonate Dehydratase (Target Efi-502209) From Caulobacter Crescentus CB15 also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Mannonate Dehydratase (Target Efi-502209) From Caulobacter Crescentus CB15 (pdb code 3vcn). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of Mannonate Dehydratase (Target Efi-502209) From Caulobacter Crescentus CB15, PDB code: 3vcn:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 3vcn

Go back to Magnesium Binding Sites List in 3vcn
Magnesium binding site 1 out of 4 in the Crystal Structure of Mannonate Dehydratase (Target Efi-502209) From Caulobacter Crescentus CB15


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Mannonate Dehydratase (Target Efi-502209) From Caulobacter Crescentus CB15 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:16.2
occ:1.00
OD2 A:ASP211 2.0 17.6 1.0
O A:HOH635 2.0 18.8 1.0
OE2 A:GLU237 2.1 18.8 1.0
OE1 A:GLU263 2.1 18.4 1.0
O A:HOH791 2.2 19.7 1.0
O2 A:CO3503 2.2 19.4 1.0
CG A:ASP211 3.0 15.6 1.0
CD A:GLU263 3.0 18.1 1.0
CD A:GLU237 3.2 16.9 1.0
C A:CO3503 3.2 22.3 1.0
OE2 A:GLU263 3.3 18.1 1.0
OD1 A:ASP211 3.4 16.5 1.0
O1 A:CO3503 3.4 24.8 1.0
NH2 A:ARG284 3.8 19.4 1.0
OE1 A:GLU237 3.9 18.2 1.0
O A:HOH608 3.9 17.9 1.0
CD2 A:HIS213 4.0 18.9 1.0
CG A:GLU237 4.0 15.8 1.0
OD2 A:ASP238 4.1 18.9 1.0
O A:HOH684 4.1 18.1 1.0
CB A:ASP211 4.3 15.8 1.0
O3 A:CO3503 4.3 22.6 1.0
CG A:GLU263 4.4 18.7 1.0
NE2 A:HIS213 4.4 17.8 1.0
NH1 A:ARG148 4.6 16.3 1.0
CG A:ASP238 4.7 16.6 1.0
OH A:TYR160 4.7 20.9 1.0
OH C:TYR76 4.7 17.2 1.0
CZ A:ARG284 4.7 17.4 1.0
CD2 A:HIS313 4.8 18.5 1.0
NE A:ARG284 4.8 16.1 1.0

Magnesium binding site 2 out of 4 in 3vcn

Go back to Magnesium Binding Sites List in 3vcn
Magnesium binding site 2 out of 4 in the Crystal Structure of Mannonate Dehydratase (Target Efi-502209) From Caulobacter Crescentus CB15


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Mannonate Dehydratase (Target Efi-502209) From Caulobacter Crescentus CB15 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg505

b:36.3
occ:1.00
O A:HOH974 2.0 34.3 1.0
O A:HOH980 2.1 37.4 1.0
O A:HOH979 2.1 39.7 1.0
O A:HOH860 2.1 27.9 1.0
O A:HOH975 2.1 36.7 1.0
O A:HOH976 2.1 36.5 1.0
O A:HOH780 4.2 24.6 1.0
OD1 A:ASP165 4.2 22.0 1.0
O A:HOH680 4.2 26.1 1.0
OD2 A:ASP165 4.3 21.6 1.0
O A:HOH770 4.5 27.3 1.0
CG A:ASP165 4.6 22.1 1.0
CZ A:PHE168 4.8 24.4 1.0
CE2 A:PHE168 4.9 19.5 1.0

Magnesium binding site 3 out of 4 in 3vcn

Go back to Magnesium Binding Sites List in 3vcn
Magnesium binding site 3 out of 4 in the Crystal Structure of Mannonate Dehydratase (Target Efi-502209) From Caulobacter Crescentus CB15


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Mannonate Dehydratase (Target Efi-502209) From Caulobacter Crescentus CB15 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg502

b:19.1
occ:1.00
OE2 C:GLU237 2.0 18.2 1.0
OD2 C:ASP211 2.1 18.7 1.0
O C:HOH660 2.1 18.2 1.0
OE1 C:GLU263 2.1 17.8 1.0
O C:HOH641 2.2 21.1 1.0
O2 C:CO3503 2.2 19.9 1.0
CG C:ASP211 3.0 16.9 1.0
CD C:GLU263 3.1 20.0 1.0
CD C:GLU237 3.1 17.1 1.0
C C:CO3503 3.2 22.1 1.0
OE2 C:GLU263 3.3 19.3 1.0
OD1 C:ASP211 3.5 18.1 1.0
O3 C:CO3503 3.5 25.7 1.0
NH2 C:ARG284 3.8 16.3 1.0
OE1 C:GLU237 3.9 17.3 1.0
O C:HOH606 3.9 18.0 1.0
CD2 C:HIS213 4.0 20.0 1.0
CG C:GLU237 4.0 15.8 1.0
O C:HOH645 4.1 17.7 1.0
OD2 C:ASP238 4.2 17.7 1.0
CB C:ASP211 4.3 15.8 1.0
O1 C:CO3503 4.3 25.6 1.0
CG C:GLU263 4.4 19.1 1.0
NH1 C:ARG148 4.5 18.9 1.0
NE2 C:HIS213 4.5 18.9 1.0
OH C:TYR160 4.7 21.3 1.0
OH A:TYR76 4.7 17.6 1.0
CG C:ASP238 4.7 16.3 1.0
CD2 C:HIS313 4.7 15.6 1.0
CZ C:ARG284 4.8 16.0 1.0
NE C:ARG284 4.8 16.9 1.0

Magnesium binding site 4 out of 4 in 3vcn

Go back to Magnesium Binding Sites List in 3vcn
Magnesium binding site 4 out of 4 in the Crystal Structure of Mannonate Dehydratase (Target Efi-502209) From Caulobacter Crescentus CB15


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Mannonate Dehydratase (Target Efi-502209) From Caulobacter Crescentus CB15 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg505

b:35.5
occ:1.00
O C:HOH968 2.0 34.3 1.0
O C:HOH933 2.0 32.5 1.0
O C:HOH969 2.1 39.9 1.0
O C:HOH824 2.2 31.7 1.0
O C:HOH797 2.2 31.1 1.0
O C:HOH967 2.3 37.7 1.0
O C:HOH983 4.1 42.9 1.0
O C:HOH985 4.1 39.5 1.0
O C:HOH764 4.2 24.7 1.0
OD1 C:ASP165 4.2 25.7 1.0
OD2 C:ASP165 4.3 24.5 1.0
O C:HOH727 4.3 25.8 1.0
O C:HOH761 4.4 27.4 1.0
CG C:ASP165 4.7 23.7 1.0
CZ C:PHE168 4.9 22.6 1.0

Reference:

Y.Patskovsky, R.Toro, R.Bhosle, B.Hillerich, R.D.Seidel, E.Washington, A.Scott Glenn, S.Chowdhury, B.Evans, J.Hammonds, W.D.Zencheck, H.J.Imker, J.A.Gerlt, S.C.Almo. Crystal Structure of Mannonate Dehydratase From Caulobacter Crescentus CB15 To Be Published.
Page generated: Mon Dec 14 08:58:34 2020

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