5M1Y
The case of 1lkr held at the PDB and its variable amino acid occupancies; re refinement of 4ow9 to correct this
Replaces: 4OW9Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003796 | molecular_function | lysozyme activity |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0005737 | cellular_component | cytoplasm |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0016231 | molecular_function | beta-N-acetylglucosaminidase activity |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0016998 | biological_process | cell wall macromolecule catabolic process |
A | 0031640 | biological_process | killing of cells of another organism |
A | 0042742 | biological_process | defense response to bacterium |
A | 0042802 | molecular_function | identical protein binding |
A | 0050829 | biological_process | defense response to Gram-negative bacterium |
A | 0050830 | biological_process | defense response to Gram-positive bacterium |
A | 0051672 | biological_process | obsolete catabolism by organism of cell wall peptidoglycan in other organism |
B | 0003796 | molecular_function | lysozyme activity |
B | 0005515 | molecular_function | protein binding |
B | 0005576 | cellular_component | extracellular region |
B | 0005615 | cellular_component | extracellular space |
B | 0005737 | cellular_component | cytoplasm |
B | 0005783 | cellular_component | endoplasmic reticulum |
B | 0016231 | molecular_function | beta-N-acetylglucosaminidase activity |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0016998 | biological_process | cell wall macromolecule catabolic process |
B | 0031640 | biological_process | killing of cells of another organism |
B | 0042742 | biological_process | defense response to bacterium |
B | 0042802 | molecular_function | identical protein binding |
B | 0050829 | biological_process | defense response to Gram-negative bacterium |
B | 0050830 | biological_process | defense response to Gram-positive bacterium |
B | 0051672 | biological_process | obsolete catabolism by organism of cell wall peptidoglycan in other organism |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue PT A 201 |
Chain | Residue |
A | HIS15 |
A | IOD203 |
A | IOD204 |
A | CL217 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue PT A 202 |
Chain | Residue |
A | IOD205 |
A | IOD206 |
A | IOD207 |
A | CL218 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue IOD A 203 |
Chain | Residue |
A | PT201 |
A | CL217 |
A | HIS15 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue IOD A 204 |
Chain | Residue |
A | HIS15 |
A | ASN93 |
A | PT201 |
A | CL217 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue IOD A 205 |
Chain | Residue |
A | ARG128 |
A | PT202 |
A | CL218 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue IOD A 206 |
Chain | Residue |
A | PT202 |
A | IOD207 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue IOD A 207 |
Chain | Residue |
A | PT202 |
A | IOD206 |
A | CL218 |
site_id | AC8 |
Number of Residues | 1 |
Details | binding site for residue IOD A 208 |
Chain | Residue |
A | IOD220 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue IOD A 209 |
Chain | Residue |
A | ASN74 |
B | LYS116 |
site_id | AD1 |
Number of Residues | 1 |
Details | binding site for residue IOD A 210 |
Chain | Residue |
B | SER81 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue IOD A 212 |
Chain | Residue |
A | SER24 |
A | GLY26 |
A | GLN121 |
A | ILE124 |
B | GLN41 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue DMS A 214 |
Chain | Residue |
A | GLN57 |
A | ILE58 |
A | ASN59 |
A | ILE98 |
A | ALA107 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue DMS A 215 |
Chain | Residue |
A | ARG5 |
A | ALA122 |
A | TRP123 |
A | ARG125 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue DMS A 216 |
Chain | Residue |
A | ASP66 |
A | SER81 |
B | ARG21 |
B | GLY22 |
B | ASN113 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue CL A 217 |
Chain | Residue |
A | PT201 |
A | IOD203 |
A | IOD204 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue CL A 218 |
Chain | Residue |
A | ARG128 |
A | PT202 |
A | IOD205 |
A | IOD207 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue IOD A 219 |
Chain | Residue |
A | ARG14 |
A | HIS15 |
A | ASP87 |
site_id | AD9 |
Number of Residues | 3 |
Details | binding site for residue IOD A 220 |
Chain | Residue |
A | LYS96 |
A | VAL109 |
A | IOD208 |
site_id | AE1 |
Number of Residues | 1 |
Details | binding site for residue IOD A 221 |
Chain | Residue |
A | TYR23 |
site_id | AE2 |
Number of Residues | 1 |
Details | binding site for residue IOD A 222 |
Chain | Residue |
A | ILE78 |
site_id | AE3 |
Number of Residues | 2 |
Details | binding site for residue IOD A 223 |
Chain | Residue |
A | TRP62 |
A | ARG73 |
site_id | AE4 |
Number of Residues | 4 |
Details | binding site for residue PT B 201 |
Chain | Residue |
B | HIS15 |
B | IOD202 |
B | IOD203 |
B | CL212 |
site_id | AE5 |
Number of Residues | 3 |
Details | binding site for residue IOD B 202 |
Chain | Residue |
B | ARG14 |
B | HIS15 |
B | PT201 |
site_id | AE6 |
Number of Residues | 4 |
Details | binding site for residue IOD B 203 |
Chain | Residue |
B | HIS15 |
B | LYS96 |
B | PT201 |
B | CL212 |
site_id | AE7 |
Number of Residues | 1 |
Details | binding site for residue IOD B 204 |
Chain | Residue |
A | LYS116 |
site_id | AE8 |
Number of Residues | 1 |
Details | binding site for residue IOD B 208 |
Chain | Residue |
B | ASN65 |
site_id | AE9 |
Number of Residues | 3 |
Details | binding site for residue DMS B 209 |
Chain | Residue |
B | ARG5 |
B | ALA122 |
B | TRP123 |
site_id | AF1 |
Number of Residues | 5 |
Details | binding site for residue DMS B 210 |
Chain | Residue |
B | ILE58 |
B | ASN59 |
B | TRP63 |
B | ALA107 |
B | TRP108 |
site_id | AF2 |
Number of Residues | 3 |
Details | binding site for residue DMS B 211 |
Chain | Residue |
B | GLN121 |
B | ILE124 |
B | ARG125 |
site_id | AF3 |
Number of Residues | 5 |
Details | binding site for residue CL B 212 |
Chain | Residue |
B | HIS15 |
B | LYS96 |
B | PT201 |
B | IOD203 |
B | NA213 |
site_id | AF4 |
Number of Residues | 1 |
Details | binding site for residue NA B 213 |
Chain | Residue |
B | CL212 |
site_id | AF5 |
Number of Residues | 1 |
Details | binding site for residue IOD B 214 |
Chain | Residue |
B | LEU129 |
site_id | AF6 |
Number of Residues | 2 |
Details | binding site for residue IOD B 215 |
Chain | Residue |
A | ASN103 |
A | ASN106 |
site_id | AF7 |
Number of Residues | 1 |
Details | binding site for residue IOD B 216 |
Chain | Residue |
B | GLY71 |
Functional Information from PROSITE/UniProt
site_id | PS00128 |
Number of Residues | 19 |
Details | GLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CnipCsaLlssDItasvnC |
Chain | Residue | Details |
A | CYS76-CYS94 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: |
Chain | Residue | Details |
A | GLU35 | |
A | ASP52 | |
B | GLU35 | |
B | ASP52 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP101 | |
B | ASP101 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 203 |
Chain | Residue | Details |
A | GLU35 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | ASN46 | |
A | ASP48 | |
A | SER50 | |
A | ASP52 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction |
A | ASN59 |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 203 |
Chain | Residue | Details |
B | GLU35 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | ASN46 | |
B | ASP48 | |
B | SER50 | |
B | ASP52 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction |
B | ASN59 |