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Chlorine in PDB 2x2h: Crystal Structure of the Gracilariopsis Lemaneiformis Alpha-1,4- Glucan Lyase

Enzymatic activity of Crystal Structure of the Gracilariopsis Lemaneiformis Alpha-1,4- Glucan Lyase

All present enzymatic activity of Crystal Structure of the Gracilariopsis Lemaneiformis Alpha-1,4- Glucan Lyase:
4.2.2.13;

Protein crystallography data

The structure of Crystal Structure of the Gracilariopsis Lemaneiformis Alpha-1,4- Glucan Lyase, PDB code: 2x2h was solved by H.J.Rozeboom, S.Yu, S.Madrid, K.H.Kalk, B.W.Dijkstra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 132.45 / 2.06
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 91.678, 96.629, 134.457, 80.54, 83.28, 85.26
R / Rfree (%) 16.8 / 21.5

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Gracilariopsis Lemaneiformis Alpha-1,4- Glucan Lyase (pdb code 2x2h). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of the Gracilariopsis Lemaneiformis Alpha-1,4- Glucan Lyase, PDB code: 2x2h:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 2x2h

Go back to Chlorine Binding Sites List in 2x2h
Chlorine binding site 1 out of 2 in the Crystal Structure of the Gracilariopsis Lemaneiformis Alpha-1,4- Glucan Lyase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the Gracilariopsis Lemaneiformis Alpha-1,4- Glucan Lyase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl2050

b:48.8
occ:1.00
N A:THR555 3.2 24.6 1.0
NE A:ARG649 3.2 22.7 1.0
OG1 A:THR555 3.2 23.2 1.0
NH2 A:ARG649 3.5 23.2 1.0
N A:VAL556 3.7 25.4 1.0
CG2 A:VAL556 3.7 25.4 1.0
CD1 A:TYR266 3.8 25.6 1.0
CZ A:ARG649 3.8 23.0 1.0
CA A:THR555 3.9 24.2 1.0
C A:MET554 4.0 25.0 1.0
CB A:THR555 4.1 24.0 1.0
CB A:ARG649 4.1 22.8 1.0
C A:THR555 4.1 24.9 1.0
O A:ARG649 4.2 22.4 1.0
CA A:MET554 4.2 25.7 1.0
CG A:ARG649 4.2 22.6 1.0
CD A:ARG649 4.2 22.3 1.0
C A:ARG649 4.3 22.8 1.0
N A:MET554 4.3 24.5 1.0
N A:GLY650 4.4 23.1 1.0
CA A:GLY650 4.4 22.8 1.0
CE1 A:TYR266 4.4 25.9 1.0
CG2 A:THR555 4.5 24.1 1.0
CA A:VAL556 4.5 25.2 1.0
CB A:VAL556 4.7 25.1 1.0
O A:TYR238 4.7 21.3 1.0
CG A:TYR266 4.8 25.1 1.0
CB A:ALA558 4.9 25.7 1.0
CB A:TYR266 4.9 23.8 1.0
CA A:ARG649 4.9 22.7 1.0

Chlorine binding site 2 out of 2 in 2x2h

Go back to Chlorine Binding Sites List in 2x2h
Chlorine binding site 2 out of 2 in the Crystal Structure of the Gracilariopsis Lemaneiformis Alpha-1,4- Glucan Lyase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of the Gracilariopsis Lemaneiformis Alpha-1,4- Glucan Lyase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl2042

b:57.0
occ:1.00
O B:HOH3416 2.7 41.6 1.0
NH2 B:ARG649 3.0 32.4 1.0
NE B:ARG649 3.0 31.3 1.0
OG1 B:THR555 3.2 31.8 1.0
CZ B:ARG649 3.5 31.9 1.0
CG2 B:VAL556 3.5 31.6 1.0
N B:THR555 3.6 32.6 1.0
CD1 B:TYR266 3.7 30.4 1.0
N B:VAL556 3.7 33.2 1.0
C B:THR555 4.1 33.3 1.0
CA B:THR555 4.1 33.1 1.0
CB B:ARG649 4.2 29.5 1.0
CB B:THR555 4.2 32.7 1.0
CD B:ARG649 4.2 30.6 1.0
CA B:GLY650 4.3 29.6 1.0
CB B:TYR266 4.3 29.5 1.0
C B:ARG649 4.3 29.3 1.0
N B:GLY650 4.3 29.4 1.0
CG B:ARG649 4.3 30.4 1.0
O B:ARG649 4.4 30.3 1.0
CA B:VAL556 4.4 32.5 1.0
O B:TYR238 4.4 27.7 1.0
CG B:TYR266 4.5 29.9 1.0
C B:MET554 4.5 34.0 1.0
CE1 B:TYR266 4.6 30.3 1.0
CB B:VAL556 4.6 32.2 1.0
NH1 B:ARG649 4.8 31.4 1.0
CA B:MET554 4.8 34.4 1.0
O B:TYR266 4.9 29.5 1.0
CA B:TYR266 4.9 29.1 1.0
CA B:ARG649 4.9 28.9 1.0
N B:MET554 4.9 34.7 1.0
O B:THR555 4.9 33.7 1.0

Reference:

H.J.Rozeboom, S.Yu, S.Madrid, K.H.Kalk, R.Zhang, B.W.Dijkstra. Crystal Structure of Alpha-1,4-Glucan Lyase, A Unique Glycoside Hydrolase Family Member with A Novel Catalytic Mechanism. J.Biol.Chem. V. 288 26764 2013.
ISSN: ISSN 0021-9258
PubMed: 23902768
DOI: 10.1074/JBC.M113.485896
Page generated: Fri Jul 11 01:45:34 2025

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