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Chlorine in PDB 1lzr: Structural Changes of the Active Site Cleft and Different Saccharide Binding Modes in Human Lysozyme Co-Crystallized with Hexa-N-Acetyl- Chitohexaose at pH 4.0

Enzymatic activity of Structural Changes of the Active Site Cleft and Different Saccharide Binding Modes in Human Lysozyme Co-Crystallized with Hexa-N-Acetyl- Chitohexaose at pH 4.0

All present enzymatic activity of Structural Changes of the Active Site Cleft and Different Saccharide Binding Modes in Human Lysozyme Co-Crystallized with Hexa-N-Acetyl- Chitohexaose at pH 4.0:
3.2.1.17;

Protein crystallography data

The structure of Structural Changes of the Active Site Cleft and Different Saccharide Binding Modes in Human Lysozyme Co-Crystallized with Hexa-N-Acetyl- Chitohexaose at pH 4.0, PDB code: 1lzr was solved by M.Matsushima, K.Inaka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 5.00 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.510, 60.910, 34.010, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structural Changes of the Active Site Cleft and Different Saccharide Binding Modes in Human Lysozyme Co-Crystallized with Hexa-N-Acetyl- Chitohexaose at pH 4.0 (pdb code 1lzr). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structural Changes of the Active Site Cleft and Different Saccharide Binding Modes in Human Lysozyme Co-Crystallized with Hexa-N-Acetyl- Chitohexaose at pH 4.0, PDB code: 1lzr:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 1lzr

Go back to Chlorine Binding Sites List in 1lzr
Chlorine binding site 1 out of 2 in the Structural Changes of the Active Site Cleft and Different Saccharide Binding Modes in Human Lysozyme Co-Crystallized with Hexa-N-Acetyl- Chitohexaose at pH 4.0


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structural Changes of the Active Site Cleft and Different Saccharide Binding Modes in Human Lysozyme Co-Crystallized with Hexa-N-Acetyl- Chitohexaose at pH 4.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl131

b:13.2
occ:0.91
 O A:HOH270 3.1 26.9 1.0
N A:SER80 3.2 8.3 1.0
O A:HOH282 3.3 17.0 0.9
CB A:SER80 3.8 9.6 1.0
CA A:LEU79 3.9 11.7 1.0
CB A:ALA83 4.0 7.8 1.0
CD2 A:LEU79 4.0 14.8 1.0
C A:LEU79 4.1 9.8 1.0
CA A:SER80 4.1 8.7 1.0
CB A:LEU79 4.4 12.4 1.0
O A:SER80 4.4 8.8 1.0
C A:SER80 4.8 9.0 1.0
CG A:LEU79 4.9 15.2 1.0
O A:HIS78 5.0 13.0 1.0
O A:HOH263 5.0 55.7 0.8
OG A:SER80 5.0 12.2 1.0

Chlorine binding site 2 out of 2 in 1lzr

Go back to Chlorine Binding Sites List in 1lzr
Chlorine binding site 2 out of 2 in the Structural Changes of the Active Site Cleft and Different Saccharide Binding Modes in Human Lysozyme Co-Crystallized with Hexa-N-Acetyl- Chitohexaose at pH 4.0


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structural Changes of the Active Site Cleft and Different Saccharide Binding Modes in Human Lysozyme Co-Crystallized with Hexa-N-Acetyl- Chitohexaose at pH 4.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl132

b:10.8
occ:0.79
 O A:HOH285 3.2 16.3 1.0
ND2 A:ASN66 3.3 11.8 1.0
CA A:SER80 3.7 8.7 1.0
CB A:ASN66 3.8 9.0 1.0
CB A:SER80 3.9 9.6 1.0
O A:HOH298 4.0 34.1 0.9
N A:SER80 4.1 8.3 1.0
CG A:ASN66 4.1 9.7 1.0
O A:ASN66 4.2 7.7 1.0
O A:HOH282 4.4 17.0 0.9
C A:LEU79 4.5 9.8 1.0
OG A:SER80 4.6 12.2 1.0
O A:LEU79 4.6 10.6 1.0
ND2 A:ASN75 4.8 13.8 1.0
C A:ASN66 4.8 7.5 1.0
CA A:ASN66 4.8 8.8 1.0
O A:HOH301 4.9 52.5 1.0

Reference:

H.Song, K.Inaka, K.Maenaka, M.Matsushima. Structural Changes of Active Site Cleft and Different Saccharide Binding Modes in Human Lysozyme Co-Crystallized with Hexa-N-Acetyl-Chitohexaose at pH 4.0. J.Mol.Biol. V. 244 522 1994.
ISSN: ISSN 0022-2836
PubMed: 7990138
DOI: 10.1006/JMBI.1994.1750
Page generated: Thu Jul 10 18:07:47 2025

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