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Chlorine in PDB 4m3k: Structure of A Single Domain Camelid Antibody Fragment Cab-H7S in Complex with the Blap Beta-Lactamase From Bacillus Licheniformis

Enzymatic activity of Structure of A Single Domain Camelid Antibody Fragment Cab-H7S in Complex with the Blap Beta-Lactamase From Bacillus Licheniformis

All present enzymatic activity of Structure of A Single Domain Camelid Antibody Fragment Cab-H7S in Complex with the Blap Beta-Lactamase From Bacillus Licheniformis:
3.5.2.6;

Protein crystallography data

The structure of Structure of A Single Domain Camelid Antibody Fragment Cab-H7S in Complex with the Blap Beta-Lactamase From Bacillus Licheniformis, PDB code: 4m3k was solved by C.Pain, F.Kerff, R.Herman, E.Sauvage, S.Preumont, P.Charlier, M.Dumoulin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.90 / 1.48
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 51.818, 42.940, 74.818, 90.00, 105.29, 90.00
R / Rfree (%) 16.1 / 19.5

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of A Single Domain Camelid Antibody Fragment Cab-H7S in Complex with the Blap Beta-Lactamase From Bacillus Licheniformis (pdb code 4m3k). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of A Single Domain Camelid Antibody Fragment Cab-H7S in Complex with the Blap Beta-Lactamase From Bacillus Licheniformis, PDB code: 4m3k:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 4m3k

Go back to Chlorine Binding Sites List in 4m3k
Chlorine binding site 1 out of 2 in the Structure of A Single Domain Camelid Antibody Fragment Cab-H7S in Complex with the Blap Beta-Lactamase From Bacillus Licheniformis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of A Single Domain Camelid Antibody Fragment Cab-H7S in Complex with the Blap Beta-Lactamase From Bacillus Licheniformis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl401

b:19.3
occ:1.00
 OH B:TYR37 2.9 17.7 1.0
O A:HOH502 3.0 14.4 1.0
O A:HOH593 3.3 26.9 1.0
NH1 B:ARG45 3.3 15.3 1.0
NZ A:LYS140 3.5 13.5 1.0
ND2 A:ASN136 3.5 12.7 1.0
CZ B:TYR37 3.5 16.1 1.0
NH2 B:ARG45 3.5 16.0 1.0
CE2 B:TYR37 3.5 16.5 1.0
CE A:LYS140 3.8 13.2 1.0
CZ B:ARG45 3.9 14.4 1.0
CG A:ASN136 3.9 11.7 1.0
O A:HOH504 3.9 14.7 1.0
CB A:ASN136 4.0 11.5 1.0
CG A:PHE165 4.3 14.2 1.0
CB A:PHE165 4.3 13.6 1.0
CD1 A:PHE165 4.3 13.1 1.0
CE1 B:TYR37 4.7 15.5 1.0
CD2 B:TYR37 4.7 16.0 1.0
CG1 A:VAL103 4.8 13.7 1.0
OD1 A:ASN136 4.8 12.5 1.0
O A:GLU166 4.9 16.1 1.0
CD2 A:PHE165 4.9 16.5 1.0
CE1 A:PHE165 4.9 13.3 1.0

Chlorine binding site 2 out of 2 in 4m3k

Go back to Chlorine Binding Sites List in 4m3k
Chlorine binding site 2 out of 2 in the Structure of A Single Domain Camelid Antibody Fragment Cab-H7S in Complex with the Blap Beta-Lactamase From Bacillus Licheniformis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of A Single Domain Camelid Antibody Fragment Cab-H7S in Complex with the Blap Beta-Lactamase From Bacillus Licheniformis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl201

b:17.7
occ:1.00
 OG B:SER53 3.0 17.8 1.0
N B:SER53 3.4 15.8 1.0
CB B:ASN52 3.5 15.1 1.0
CB B:SER53 3.6 17.6 1.0
CA B:THR32 3.7 15.4 1.0
CA A:GLY143 3.8 13.9 1.0
O B:THR32 3.8 17.0 1.0
CB B:THR32 3.8 15.1 1.0
C B:THR32 3.9 15.4 1.0
CG B:ASN52 4.0 15.5 1.0
CA B:SER53 4.1 16.7 1.0
CG2 B:THR32 4.2 16.1 1.0
ND2 B:ASN52 4.3 15.9 1.0
C B:ASN52 4.3 15.4 1.0
CA B:ASN52 4.4 14.6 1.0
O B:HOH334 4.5 24.1 1.0
N A:GLY143 4.7 13.0 1.0
OD1 B:ASN52 4.7 15.8 1.0
O A:GLY143 4.7 15.4 1.0
O A:HOH551 4.8 26.2 1.0
N B:VAL54 4.8 18.0 1.0
O B:ILE31 4.8 16.9 1.0
C A:GLY143 4.8 13.5 1.0
N B:THR33 4.8 15.0 1.0
C B:SER53 4.9 17.5 1.0
OG A:SER147 4.9 18.1 1.0

Reference:

C.Pain, A.Cosolo, S.Preumont, N.Scarafone, D.Thorn, R.Herman, H.Spiegel, E.Pardon, A.Matagne, P.Charlier, J.Steyaert, C.Damblon, F.Kerff, G.Esposito, M.Dumoulin. Probing the Mechanism of Aggregation of Polyq Model Proteins with Camelid Heavy-Chain Antibody Fragments To Be Published.
Page generated: Sun Jul 21 19:32:09 2024

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