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Chlorine in PDB 3sds: Crystal Structure of A Mitochondrial Ornithine Carbamoyltransferase From Coccidioides Immitis

Enzymatic activity of Crystal Structure of A Mitochondrial Ornithine Carbamoyltransferase From Coccidioides Immitis

All present enzymatic activity of Crystal Structure of A Mitochondrial Ornithine Carbamoyltransferase From Coccidioides Immitis:
2.1.3.3;

Protein crystallography data

The structure of Crystal Structure of A Mitochondrial Ornithine Carbamoyltransferase From Coccidioides Immitis, PDB code: 3sds was solved by T.E.Edwards, J.Abendroth, Seattle Structural Genomics Center Forinfectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.80
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 150.360, 150.360, 92.110, 90.00, 90.00, 120.00
R / Rfree (%) 19.3 / 23.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of A Mitochondrial Ornithine Carbamoyltransferase From Coccidioides Immitis (pdb code 3sds). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 6 binding sites of Chlorine where determined in the Crystal Structure of A Mitochondrial Ornithine Carbamoyltransferase From Coccidioides Immitis, PDB code: 3sds:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6;

Chlorine binding site 1 out of 6 in 3sds

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Chlorine binding site 1 out of 6 in the Crystal Structure of A Mitochondrial Ornithine Carbamoyltransferase From Coccidioides Immitis


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 A Mitochondrial Ornithine Carbamoyltransferase From Coccidioides Immitis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl350

b:78.7
occ:1.00
 N A:LYS96 3.5 59.7 1.0
N A:ARG72 3.6 57.4 1.0
C A:LYS71 3.7 56.6 1.0
CA A:ARG72 3.7 56.5 1.0
O A:LYS71 3.7 55.3 1.0
CA A:GLY95 3.9 54.4 1.0
CG A:LYS96 3.9 65.8 1.0
O A:PHE69 3.9 54.5 1.0
CZ A:PHE93 4.2 47.2 1.0
C A:GLY95 4.2 57.4 1.0
CB A:PHE69 4.3 49.9 1.0
CB A:LYS96 4.3 63.3 1.0
CA A:LYS71 4.5 57.7 1.0
C A:PHE69 4.5 52.9 1.0
CA A:LYS96 4.5 62.9 1.0
NZ A:LYS96 4.5 72.5 1.0
CB A:ARG72 4.6 57.3 1.0
N A:LYS71 4.6 56.8 1.0
CE1 A:PHE93 4.7 47.0 1.0
C A:ARG72 4.7 55.0 1.0
C A:SER70 4.9 57.7 1.0
N A:SER73 4.9 53.8 1.0

Chlorine binding site 2 out of 6 in 3sds

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Chlorine binding site 2 out of 6 in the Crystal Structure of A Mitochondrial Ornithine Carbamoyltransferase From Coccidioides Immitis


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 A Mitochondrial Ornithine Carbamoyltransferase From Coccidioides Immitis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl351

b:71.9
occ:0.33
 ND1 A:HIS90 3.1 41.0 1.0
CE1 A:HIS90 3.8 42.6 1.0
CG A:HIS90 4.2 40.7 1.0
CB A:HIS90 4.6 39.2 1.0
NE2 A:HIS90 5.0 42.2 1.0

Chlorine binding site 3 out of 6 in 3sds

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Chlorine binding site 3 out of 6 in the Crystal Structure of A Mitochondrial Ornithine Carbamoyltransferase From Coccidioides Immitis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of A Mitochondrial Ornithine Carbamoyltransferase From Coccidioides Immitis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl350

b:66.3
occ:1.00
 N B:LYS96 3.6 59.3 1.0
CG B:LYS96 3.7 63.9 1.0
CZ B:PHE93 3.9 47.3 1.0
CA B:ARG72 3.9 56.3 1.0
CA B:GLY95 3.9 54.1 1.0
N B:ARG72 4.0 57.2 1.0
C B:LYS71 4.1 56.5 1.0
O B:LYS71 4.1 55.1 1.0
O B:PHE69 4.2 54.4 1.0
C B:GLY95 4.2 57.4 1.0
CD B:LYS96 4.4 65.4 1.0
CB B:LYS96 4.4 63.4 1.0
CE1 B:PHE93 4.5 47.4 1.0
CA B:LYS96 4.6 62.6 1.0
CB B:ARG72 4.7 57.0 1.0
CB B:PHE69 4.7 50.8 1.0
C B:PHE69 4.9 53.3 1.0
CE B:LYS96 4.9 67.0 1.0
CA B:LYS71 5.0 57.7 1.0
CE2 B:PHE93 5.0 47.8 1.0

Chlorine binding site 4 out of 6 in 3sds

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Chlorine binding site 4 out of 6 in the Crystal Structure of A Mitochondrial Ornithine Carbamoyltransferase From Coccidioides Immitis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of A Mitochondrial Ornithine Carbamoyltransferase From Coccidioides Immitis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl351

b:65.7
occ:0.33
 ND1 B:HIS90 4.1 41.7 1.0
CE1 B:HIS90 4.8 43.2 1.0

Chlorine binding site 5 out of 6 in 3sds

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Chlorine binding site 5 out of 6 in the Crystal Structure of A Mitochondrial Ornithine Carbamoyltransferase From Coccidioides Immitis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Crystal Structure of A Mitochondrial Ornithine Carbamoyltransferase From Coccidioides Immitis within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl350

b:54.8
occ:1.00
 N C:LYS96 3.2 62.0 1.0
O C:LYS71 3.6 58.2 1.0
C C:LYS71 3.7 59.7 1.0
CB C:LYS96 3.7 66.4 1.0
N C:ARG72 3.7 60.0 1.0
CA C:ARG72 3.8 58.7 1.0
CA C:LYS96 4.0 65.5 1.0
CA C:GLY95 4.0 56.2 1.0
O C:PHE69 4.1 56.8 1.0
C C:GLY95 4.1 59.6 1.0
CZ C:PHE93 4.2 47.5 1.0
CB C:PHE69 4.4 52.6 1.0
CA C:LYS71 4.4 61.5 1.0
CB C:ARG72 4.6 59.8 1.0
N C:LYS71 4.6 60.4 1.0
C C:PHE69 4.7 55.7 1.0
CE1 C:PHE93 4.8 46.5 1.0
C C:ARG72 4.9 57.4 1.0
C C:SER70 4.9 61.6 1.0

Chlorine binding site 6 out of 6 in 3sds

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Chlorine binding site 6 out of 6 in the Crystal Structure of A Mitochondrial Ornithine Carbamoyltransferase From Coccidioides Immitis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Crystal Structure of A Mitochondrial Ornithine Carbamoyltransferase From Coccidioides Immitis within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl351

b:65.0
occ:0.33
 ND1 C:HIS90 3.4 42.4 1.0
CE1 C:HIS90 4.2 42.9 1.0
CG C:HIS90 4.5 40.9 1.0
CB C:HIS90 4.7 39.8 1.0
CA C:HIS90 5.0 38.9 1.0

Reference:

S.N.Hewitt, R.Choi, A.Kelley, G.J.Crowther, A.J.Napuli, W.C.Van Voorhis. Expression of Proteins in Escherichia Coli As Fusions with Maltose-Binding Protein to Rescue Non-Expressed Targets in A High-Throughput Protein-Expression and Purification Pipeline. Acta Crystallogr.,Sect.F V. 67 1006 2011.
ISSN: ESSN 1744-3091
PubMed: 21904041
DOI: 10.1107/S1744309111022159
Page generated: Fri Jul 11 10:14:39 2025

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