Atomistry » Calcium » PDB 1spu-1t5s » 1t1g
Atomistry »
  Calcium »
    PDB 1spu-1t5s »
      1t1g »

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: Tue Jul 8 02:09:33 2025

Last articles

Mg in 5MH5
Mg in 5MGY
Mg in 5MFM
Mg in 5MH1
Mg in 5MGA
Mg in 5M73
Mg in 5MFL
Mg in 5MF4
Mg in 5MF5
Mg in 5MCP
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy