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Atomistry » Calcium » PDB 4iai-4iun » 4ipm » |
Calcium in PDB 4ipm: Crystal Structure of A GH7 Family Cellobiohydrolase From Limnoria Quadripunctata in Complex with ThiocellobioseEnzymatic activity of Crystal Structure of A GH7 Family Cellobiohydrolase From Limnoria Quadripunctata in Complex with Thiocellobiose
All present enzymatic activity of Crystal Structure of A GH7 Family Cellobiohydrolase From Limnoria Quadripunctata in Complex with Thiocellobiose:
3.2.1.91; Protein crystallography data
The structure of Crystal Structure of A GH7 Family Cellobiohydrolase From Limnoria Quadripunctata in Complex with Thiocellobiose, PDB code: 4ipm
was solved by
J.E.Mcgeehan,
R.N.A.Martin,
S.D.Streeter,
S.M.Cragg,
M.J.Guille,
K.M.Schnorr,
M.Kern,
N.C.Bruce,
S.J.Mcqueen-Mason,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of A GH7 Family Cellobiohydrolase From Limnoria Quadripunctata in Complex with Thiocellobiose
(pdb code 4ipm). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of A GH7 Family Cellobiohydrolase From Limnoria Quadripunctata in Complex with Thiocellobiose, PDB code: 4ipm: Calcium binding site 1 out of 1 in 4ipmGo back to Calcium Binding Sites List in 4ipm
Calcium binding site 1 out
of 1 in the Crystal Structure of A GH7 Family Cellobiohydrolase From Limnoria Quadripunctata in Complex with Thiocellobiose
Mono view Stereo pair view
Reference:
M.Kern,
J.E.Mcgeehan,
S.D.Streeter,
R.N.Martin,
K.Besser,
L.Elias,
W.Eborall,
G.P.Malyon,
C.M.Payne,
M.E.Himmel,
K.Schnorr,
G.T.Beckham,
S.M.Cragg,
N.C.Bruce,
S.J.Mcqueen-Mason.
Structural Characterization of A Unique Marine Animal Family 7 Cellobiohydrolase Suggests A Mechanism of Cellulase Salt Tolerance. Proc.Natl.Acad.Sci.Usa V. 110 10189 2013.
Page generated: Sun Jul 14 08:16:46 2024
ISSN: ISSN 0027-8424 PubMed: 23733951 DOI: 10.1073/PNAS.1301502110 |
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