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Cobalt in PDB 3mgw: Thermodynamics and Structure of A Salmon Cold-Active Goose-Type Lysozyme

Enzymatic activity of Thermodynamics and Structure of A Salmon Cold-Active Goose-Type Lysozyme

All present enzymatic activity of Thermodynamics and Structure of A Salmon Cold-Active Goose-Type Lysozyme:
3.2.1.17;

Protein crystallography data

The structure of Thermodynamics and Structure of A Salmon Cold-Active Goose-Type Lysozyme, PDB code: 3mgw was solved by P.Kyomuhendo, B.Myrnes, B.O.Brandsdal, A.O.Smalas, I.W.Nilsen, R.Helland, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.76 / 1.75
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 103.150, 103.150, 48.670, 90.00, 90.00, 120.00
R / Rfree (%) 17.6 / 21.5

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Thermodynamics and Structure of A Salmon Cold-Active Goose-Type Lysozyme (pdb code 3mgw). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Thermodynamics and Structure of A Salmon Cold-Active Goose-Type Lysozyme, PDB code: 3mgw:

Cobalt binding site 1 out of 1 in 3mgw

Go back to Cobalt Binding Sites List in 3mgw
Cobalt binding site 1 out of 1 in the Thermodynamics and Structure of A Salmon Cold-Active Goose-Type Lysozyme


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Thermodynamics and Structure of A Salmon Cold-Active Goose-Type Lysozyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co186

b:25.5
occ:1.00
ND1 A:HIS5 2.1 25.7 1.0
N A:HIS5 2.2 27.6 1.0
CA A:HIS5 3.1 28.7 1.0
CE1 A:HIS5 3.1 30.1 1.0
CG A:HIS5 3.1 29.5 1.0
CB A:HIS5 3.4 28.4 1.0
NE2 A:HIS5 4.2 31.9 1.0
CD2 A:HIS5 4.2 30.2 1.0
C A:HIS5 4.5 28.8 1.0

Reference:

P.Kyomuhendo, B.Myrnes, B.O.Brandsdal, A.O.Smalas, I.W.Nilsen, R.Helland. Thermodynamics and Structure of A Salmon Cold Active Goose-Type Lysozyme Comp.Biochem.Physiol. B: V. 156 254 2010BIOCHEM.Mol.Biol..
ISSN: ISSN 0305-0491
PubMed: 20398783
DOI: 10.1016/J.CBPB.2010.04.002
Page generated: Sun Dec 13 10:41:31 2020

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