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Calcium in PDB 1egq: Enhancement of Enzyme Activity Through Three-Phase Partitioning: Crystal Structure of A Modified Serine Proteinase at 1.5 A Resolution

Enzymatic activity of Enhancement of Enzyme Activity Through Three-Phase Partitioning: Crystal Structure of A Modified Serine Proteinase at 1.5 A Resolution

All present enzymatic activity of Enhancement of Enzyme Activity Through Three-Phase Partitioning: Crystal Structure of A Modified Serine Proteinase at 1.5 A Resolution:
3.4.21.64;

Protein crystallography data

The structure of Enhancement of Enzyme Activity Through Three-Phase Partitioning: Crystal Structure of A Modified Serine Proteinase at 1.5 A Resolution, PDB code: 1egq was solved by R.K.Singh, S.Gourinath, S.Sharma, I.Ray, M.N.Gupta, T.P.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.55
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 68.290, 68.290, 106.360, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 20.6

Calcium Binding Sites:

The binding sites of Calcium atom in the Enhancement of Enzyme Activity Through Three-Phase Partitioning: Crystal Structure of A Modified Serine Proteinase at 1.5 A Resolution (pdb code 1egq). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Enhancement of Enzyme Activity Through Three-Phase Partitioning: Crystal Structure of A Modified Serine Proteinase at 1.5 A Resolution, PDB code: 1egq:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1egq

Go back to Calcium Binding Sites List in 1egq
Calcium binding site 1 out of 2 in the Enhancement of Enzyme Activity Through Three-Phase Partitioning: Crystal Structure of A Modified Serine Proteinase at 1.5 A Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Enhancement of Enzyme Activity Through Three-Phase Partitioning: Crystal Structure of A Modified Serine Proteinase at 1.5 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca280

b:11.7
occ:1.00
 O A:PRO175 2.5 13.7 1.0
O A:VAL177 2.5 12.8 1.0
OD1 A:ASP200 2.5 13.3 1.0
O A:HOH504 2.6 14.6 1.0
O A:HOH502 2.6 19.0 1.0
O A:HOH503 2.7 16.3 1.0
O A:HOH501 2.7 17.7 1.0
OD2 A:ASP200 2.7 14.5 1.0
CG A:ASP200 2.9 13.6 1.0
C A:PRO175 3.5 13.6 1.0
C A:VAL177 3.7 12.5 1.0
CA A:PRO175 4.2 13.7 1.0
N A:VAL177 4.2 13.1 1.0
O A:VAL198 4.3 16.1 1.0
CB A:ASP200 4.4 13.1 1.0
O A:HOH581 4.4 55.2 1.0
O A:GLU174 4.5 13.7 1.0
C A:SER176 4.5 13.4 1.0
CA A:CYS178 4.5 11.9 1.0
N A:SER176 4.5 13.1 1.0
N A:CYS178 4.6 11.9 1.0
N A:THR179 4.6 11.7 1.0
O A:HOH701 4.6 42.9 1.0
CA A:VAL177 4.7 12.7 1.0
O A:HOH605 4.7 30.8 1.0
O A:HOH509 4.7 19.9 1.0
CA A:SER176 4.8 13.5 1.0
OG1 A:THR179 4.8 12.5 1.0
SG A:CYS249 4.9 12.6 1.0

Calcium binding site 2 out of 2 in 1egq

Go back to Calcium Binding Sites List in 1egq
Calcium binding site 2 out of 2 in the Enhancement of Enzyme Activity Through Three-Phase Partitioning: Crystal Structure of A Modified Serine Proteinase at 1.5 A Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Enhancement of Enzyme Activity Through Three-Phase Partitioning: Crystal Structure of A Modified Serine Proteinase at 1.5 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca281

b:15.1
occ:0.50
 O A:THR16 2.5 21.9 1.0
OD1 A:ASP260 2.7 23.8 1.0
OD2 A:ASP260 2.7 24.2 1.0
O A:HOH506 2.9 46.0 1.0
O A:HOH505 2.9 38.6 1.0
CG A:ASP260 3.0 23.0 1.0
C A:THR16 3.7 21.6 1.0
OG1 A:THR16 3.7 25.5 1.0
O A:HOH712 3.8 94.0 1.0
CB A:ASP260 4.3 21.5 1.0
CA A:THR16 4.6 21.5 1.0
N A:SER17 4.6 21.8 1.0
CB A:THR16 4.6 22.2 1.0
CA A:SER17 4.6 22.2 1.0
ND2 A:ASN257 4.7 16.6 1.0
NH2 A:ARG12 4.8 14.9 1.0
CG A:ASN257 5.0 17.1 1.0
CG2 A:THR16 5.0 22.2 1.0

Reference:

R.K.Singh, S.Gourinath, S.Sharma, I.Roy, M.N.Gupta, C.Betzel, A.Srinivasan, T.P.Singh. Enhancement of Enzyme Activity Through Three-Phase Partitioning: Crystal Structure of A Modified Serine Proteinase at 1.5 A Resolution. Protein Eng. V. 14 307 2001.
ISSN: ISSN 0269-2139
PubMed: 11438752
DOI: 10.1093/PROTEIN/14.5.307
Page generated: Sat Dec 12 02:54:12 2020

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