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Calcium in PDB 1t1g: High Resolution Crystal Structure of Mutant E23A of Kumamolisin, A Sedolisin Type Proteinase (Previously Called Kumamolysin or Kscp)

Protein crystallography data

The structure of High Resolution Crystal Structure of Mutant E23A of Kumamolisin, A Sedolisin Type Proteinase (Previously Called Kumamolysin or Kscp), PDB code: 1t1g was solved by M.Comellas-Bigler, K.Maskos, R.Huber, H.Oyama, K.Oda, W.Bode, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.18
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.720, 78.570, 49.990, 90.00, 106.48, 90.00
R / Rfree (%) 20.2 / 22.2

Calcium Binding Sites:

The binding sites of Calcium atom in the High Resolution Crystal Structure of Mutant E23A of Kumamolisin, A Sedolisin Type Proteinase (Previously Called Kumamolysin or Kscp) (pdb code 1t1g). 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 High Resolution Crystal Structure of Mutant E23A of Kumamolisin, A Sedolisin Type Proteinase (Previously Called Kumamolysin or Kscp), PDB code: 1t1g:

Calcium binding site 1 out of 1 in 1t1g

Go back to Calcium Binding Sites List in 1t1g
Calcium binding site 1 out of 1 in the High Resolution Crystal Structure of Mutant E23A of Kumamolisin, A Sedolisin Type Proteinase (Previously Called Kumamolysin or Kscp)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of High Resolution Crystal Structure of Mutant E23A of Kumamolisin, A Sedolisin Type Proteinase (Previously Called Kumamolysin or Kscp) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca365

b:10.6
occ:1.00
O A:GLY336 2.4 11.2 1.0
OD2 A:ASP338 2.4 11.0 1.0
OD1 A:ASP316 2.4 13.2 1.0
O A:ILE317 2.5 12.7 1.0
O A:GLY334 2.5 11.4 1.0
O A:HOH368 2.6 12.1 1.0
CG A:ASP338 3.5 9.5 1.0
C A:ILE317 3.5 13.2 1.0
C A:GLY336 3.6 11.2 1.0
CG A:ASP316 3.6 13.8 1.0
C A:GLY334 3.7 11.6 1.0
N A:ILE317 3.9 13.5 1.0
N A:GLY336 3.9 11.2 1.0
OD2 A:ASP316 4.1 14.1 1.0
OG1 A:THR341 4.1 9.5 1.0
N A:GLY334 4.2 10.7 1.0
C A:PRO335 4.2 11.7 1.0
O A:GLY342 4.2 9.2 1.0
CB A:ASP338 4.3 9.2 1.0
CA A:GLY336 4.3 11.3 1.0
CA A:ILE317 4.3 12.5 1.0
OD1 A:ASP338 4.4 9.9 1.0
N A:ASP338 4.4 9.7 1.0
N A:THR318 4.5 12.2 1.0
CA A:PRO335 4.5 12.2 1.0
C A:TRP337 4.5 10.3 1.0
N A:PRO335 4.6 12.4 1.0
CA A:THR318 4.6 12.8 1.0
N A:TRP337 4.6 10.2 1.0
C A:ASP316 4.6 14.2 1.0
CG2 A:THR318 4.6 13.7 1.0
CA A:GLY334 4.6 11.3 1.0
O A:PRO335 4.7 12.0 1.0
CA A:TRP337 4.7 10.3 1.0
CB A:ASP316 4.8 12.8 1.0
CA A:ASP316 4.8 13.3 1.0
CB A:ILE317 4.8 13.0 1.0

Reference:

M.Comellas-Bigler, K.Maskos, R.Huber, H.Oyama, K.Oda, W.Bode. 1.2 A Crystal Structure of the Serine Carboxyl Proteinase Pro-Kumamolisin: Structure of An Intact Pro-Subtilase Structure V. 12 1313 2004.
ISSN: ISSN 0969-2126
PubMed: 15242607
DOI: 10.1016/J.STR.2004.04.013
Page generated: Sat Dec 12 03:20:32 2020

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