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Cobalt in PDB 3gxk: The Crystal Structure of G-Type Lysozyme From Atlantic Cod (Gadus Morhua L.) in Complex with Nag Oligomers Sheds New Light on Substrate Binding and the Catalytic Mechanism. Native Structure to 1.9

Enzymatic activity of The Crystal Structure of G-Type Lysozyme From Atlantic Cod (Gadus Morhua L.) in Complex with Nag Oligomers Sheds New Light on Substrate Binding and the Catalytic Mechanism. Native Structure to 1.9

All present enzymatic activity of The Crystal Structure of G-Type Lysozyme From Atlantic Cod (Gadus Morhua L.) in Complex with Nag Oligomers Sheds New Light on Substrate Binding and the Catalytic Mechanism. Native Structure to 1.9:
3.2.1.17;

Protein crystallography data

The structure of The Crystal Structure of G-Type Lysozyme From Atlantic Cod (Gadus Morhua L.) in Complex with Nag Oligomers Sheds New Light on Substrate Binding and the Catalytic Mechanism. Native Structure to 1.9, PDB code: 3gxk was solved by R.Helland, R.L.Larsen, S.Finstad, P.Kyomuhendo, A.N.Larsen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.02 / 1.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 110.120, 75.390, 78.370, 90.00, 92.92, 90.00
R / Rfree (%) 19.1 / 25.1

Cobalt Binding Sites:

The binding sites of Cobalt atom in the The Crystal Structure of G-Type Lysozyme From Atlantic Cod (Gadus Morhua L.) in Complex with Nag Oligomers Sheds New Light on Substrate Binding and the Catalytic Mechanism. Native Structure to 1.9 (pdb code 3gxk). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the The Crystal Structure of G-Type Lysozyme From Atlantic Cod (Gadus Morhua L.) in Complex with Nag Oligomers Sheds New Light on Substrate Binding and the Catalytic Mechanism. Native Structure to 1.9, PDB code: 3gxk:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 3gxk

Go back to Cobalt Binding Sites List in 3gxk
Cobalt binding site 1 out of 2 in the The Crystal Structure of G-Type Lysozyme From Atlantic Cod (Gadus Morhua L.) in Complex with Nag Oligomers Sheds New Light on Substrate Binding and the Catalytic Mechanism. Native Structure to 1.9


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of The Crystal Structure of G-Type Lysozyme From Atlantic Cod (Gadus Morhua L.) in Complex with Nag Oligomers Sheds New Light on Substrate Binding and the Catalytic Mechanism. Native Structure to 1.9 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Co200

b:29.4
occ:0.50
ND1 B:HIS35 2.1 20.9 1.0
CG B:HIS35 3.0 14.1 1.0
CE1 B:HIS35 3.0 22.2 1.0
CB B:HIS35 3.3 13.1 1.0
CD2 B:HIS35 4.1 17.1 1.0
NE2 B:HIS35 4.1 21.6 1.0
CD1 B:TRP183 4.4 16.8 1.0
CA B:HIS35 4.8 11.9 1.0
NE1 B:TRP183 5.0 18.1 1.0

Cobalt binding site 2 out of 2 in 3gxk

Go back to Cobalt Binding Sites List in 3gxk
Cobalt binding site 2 out of 2 in the The Crystal Structure of G-Type Lysozyme From Atlantic Cod (Gadus Morhua L.) in Complex with Nag Oligomers Sheds New Light on Substrate Binding and the Catalytic Mechanism. Native Structure to 1.9


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of The Crystal Structure of G-Type Lysozyme From Atlantic Cod (Gadus Morhua L.) in Complex with Nag Oligomers Sheds New Light on Substrate Binding and the Catalytic Mechanism. Native Structure to 1.9 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Co200

b:25.2
occ:0.30
OE2 D:GLU106 2.1 24.1 1.0
ND1 C:HIS35 2.2 25.3 1.0
CD D:GLU106 2.9 25.1 1.0
OE1 D:GLU106 3.1 26.2 1.0
CE1 C:HIS35 3.1 24.0 1.0
CG C:HIS35 3.2 20.9 1.0
CB C:HIS35 3.5 16.5 1.0
NE2 C:HIS35 4.2 24.4 1.0
CD2 C:HIS35 4.3 20.8 1.0
CG D:GLU106 4.3 22.7 1.0
CA C:ARG32 4.9 15.8 1.0
O C:VAL31 4.9 14.4 1.0
CD1 C:TRP183 5.0 20.6 1.0

Reference:

R.Helland, R.L.Larsen, S.Finstad, P.Kyomuhendo, A.N.Larsen. Crystal Structures of G-Type Lysozyme From Atlantic Cod Shed New Light on Substrate Binding and the Catalytic Mechanism. Cell.Mol.Life Sci. V. 66 2585 2009.
ISSN: ISSN 1420-682X
PubMed: 19543850
DOI: 10.1007/S00018-009-0063-X
Page generated: Sun Dec 13 10:40:35 2020

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