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Chlorine in PDB 1tzm: Crystal Structure of Acc Deaminase Complexed with Substrate Analog B- Chloro-D-Alanine

Enzymatic activity of Crystal Structure of Acc Deaminase Complexed with Substrate Analog B- Chloro-D-Alanine

All present enzymatic activity of Crystal Structure of Acc Deaminase Complexed with Substrate Analog B- Chloro-D-Alanine:
3.5.99.7;

Protein crystallography data

The structure of Crystal Structure of Acc Deaminase Complexed with Substrate Analog B- Chloro-D-Alanine, PDB code: 1tzm was solved by S.Karthikeyan, Q.Zhou, Z.Zhao, C.L.Kao, Z.Tao, H.Robinson, H.W.Liu, H.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.86 / 2.08
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 67.640, 68.263, 349.748, 90.00, 90.00, 90.00
R / Rfree (%) 22.6 / 26.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Acc Deaminase Complexed with Substrate Analog B- Chloro-D-Alanine (pdb code 1tzm). 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 Acc Deaminase Complexed with Substrate Analog B- Chloro-D-Alanine, PDB code: 1tzm:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 1tzm

Go back to Chlorine Binding Sites List in 1tzm
Chlorine binding site 1 out of 2 in the Crystal Structure of Acc Deaminase Complexed with Substrate Analog B- Chloro-D-Alanine


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 Acc Deaminase Complexed with Substrate Analog B- Chloro-D-Alanine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl501

b:40.0
occ:0.50
CL A:C2N501 0.0 40.0 0.5
O A:HOH801 0.9 17.8 0.5
CB A:C2N501 1.8 40.5 0.5
OAD A:NAK601 2.1 40.7 0.5
CA A:C2N501 2.7 40.9 0.5
N A:C2N501 3.1 38.7 0.5
O A:ILE73 3.1 31.7 1.0
N A:GLY161 3.1 39.4 1.0
CAF A:NAK601 3.2 38.7 0.5
CA A:ALA160 3.5 39.2 1.0
CB A:ALA160 3.5 39.0 1.0
CA A:GLY74 3.6 29.3 1.0
CZ3 A:TRP102 3.7 51.5 1.0
CH2 A:TRP102 3.7 51.5 1.0
C A:ALA160 3.8 40.2 1.0
OAC A:NAK601 4.0 37.8 0.5
CB A:GLN80 4.0 34.2 1.0
C A:ILE73 4.0 29.4 1.0
CAE A:NAK601 4.1 39.0 0.5
C A:C2N501 4.1 40.5 0.5
CA A:GLY161 4.1 39.2 1.0
CAG A:NAK601 4.1 37.7 0.5
O A:HOH1197 4.1 45.7 1.0
OG A:SER78 4.2 39.3 1.0
CG A:GLN80 4.2 36.4 1.0
N A:GLY74 4.3 28.6 1.0
O A:HOH876 4.3 35.7 1.0
CG2 A:THR199 4.6 36.1 1.0
O A:C2N501 4.7 41.8 0.5
OXT A:C2N501 4.7 41.6 0.5
N A:ALA160 4.9 40.1 1.0
C A:GLY74 4.9 30.5 1.0
CE3 A:TRP102 4.9 50.8 1.0
O A:ALA160 4.9 38.2 1.0
CB A:SER78 5.0 35.5 1.0
CZ2 A:TRP102 5.0 51.0 1.0

Chlorine binding site 2 out of 2 in 1tzm

Go back to Chlorine Binding Sites List in 1tzm
Chlorine binding site 2 out of 2 in the Crystal Structure of Acc Deaminase Complexed with Substrate Analog B- Chloro-D-Alanine


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 Acc Deaminase Complexed with Substrate Analog B- Chloro-D-Alanine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl502

b:44.1
occ:0.50
CL C:C2N502 0.0 44.1 0.5
O C:HOH802 0.6 37.0 0.5
CB C:C2N502 1.8 44.4 0.5
CA C:C2N502 2.7 43.3 0.5
OAD C:NAK602 2.8 34.4 0.5
N C:GLY75 3.2 26.7 1.0
C C:C2N502 3.2 43.6 0.5
CAF C:NAK602 3.4 32.5 0.5
CB C:SER78 3.4 29.4 1.0
OXT C:C2N502 3.5 41.6 0.5
OH C:TYR268 3.6 32.0 1.0
OG C:SER78 3.6 28.8 1.0
OAC C:NAK602 3.6 36.5 0.5
CA C:SER78 3.7 29.9 1.0
OH C:TYR294 3.8 33.6 1.0
CA C:GLY74 3.9 28.1 1.0
CZ3 C:TRP102 3.9 43.9 1.0
CE3 C:TRP102 3.9 42.0 1.0
CA C:GLY75 4.0 25.9 1.0
C C:GLY74 4.0 27.9 1.0
N C:C2N502 4.0 43.0 0.5
O C:C2N502 4.0 45.1 0.5
N C:SER78 4.4 29.2 1.0
O C:HOH907 4.4 37.8 1.0
CAG C:NAK602 4.5 31.5 0.5
CZ C:TYR268 4.6 35.7 1.0
O C:GLY75 4.7 26.0 1.0
C C:GLY75 4.7 26.8 1.0
CAE C:NAK602 4.9 28.6 0.5
C C:SER78 4.9 28.8 1.0

Reference:

S.Karthikeyan, Q.Zhou, Z.Zhao, C.L.Kao, Z.Tao, H.Robinson, H.W.Liu, H.Zhang. Structural Analysis of Pseudomonas 1-Aminocyclopropane-1-Carboxylate Deaminase Complexes: Insight Into the Mechanism of A Unique Pyridoxal-5'-Phosphate Dependent Cyclopropane Ring-Opening Reaction Biochemistry V. 43 13328 2004.
ISSN: ISSN 0006-2960
PubMed: 15491139
DOI: 10.1021/BI048878G
Page generated: Thu Jul 10 19:39:50 2025

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