6RO5
1Yr-Y: Lysozyme with Re Cluster 1 year on shelf
Functional 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 | 2 |
Details | binding site for residue RE A 201 |
Chain | Residue |
A | RE202 |
B | RRE210 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue RE A 202 |
Chain | Residue |
A | RE201 |
B | RRE210 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue CL A 203 |
Chain | Residue |
A | TYR23 |
B | ASN113 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue CL A 204 |
Chain | Residue |
A | ASN65 |
A | THR69 |
A | HOH315 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue NA A 205 |
Chain | Residue |
A | SER60 |
A | CYS64 |
A | SER72 |
A | ARG73 |
A | HOH315 |
A | HOH316 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue ACT A 206 |
Chain | Residue |
A | ILE58 |
A | ASN59 |
A | TRP63 |
A | ALA107 |
A | TRP108 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue RE A 207 |
Chain | Residue |
A | GLU35 |
A | HOH304 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue RE A 208 |
Chain | Residue |
A | ASP119 |
A | ARG125 |
A | HOH317 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue RE A 209 |
Chain | Residue |
A | ASP18 |
A | HOH324 |
A | HOH325 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue RE A 210 |
Chain | Residue |
A | ASN46 |
A | ASP52 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue RE A 211 |
Chain | Residue |
A | LEU129 |
A | QEB212 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue QEB A 212 |
Chain | Residue |
A | LEU129 |
A | RE211 |
B | ASP48 |
B | PRO70 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue QEB A 213 |
Chain | Residue |
A | ARG5 |
A | TRP123 |
A | HOH321 |
site_id | AD5 |
Number of Residues | 1 |
Details | binding site for residue QEB A 214 |
Chain | Residue |
A | HOH323 |
site_id | AD6 |
Number of Residues | 7 |
Details | binding site for residue QEB A 215 |
Chain | Residue |
A | ARG61 |
A | GLY71 |
A | HOH301 |
A | HOH305 |
B | ASP18 |
B | HOH303 |
B | HOH318 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue QEB A 216 |
Chain | Residue |
A | ASP48 |
A | ARG61 |
A | THR69 |
A | PRO70 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue RRE A 218 |
Chain | Residue |
A | ALA11 |
A | ARG14 |
A | HIS15 |
A | ASP87 |
A | ILE88 |
A | THR89 |
site_id | AD9 |
Number of Residues | 1 |
Details | binding site for residue RE B 201 |
Chain | Residue |
B | LEU129 |
site_id | AE1 |
Number of Residues | 2 |
Details | binding site for residue RE B 202 |
Chain | Residue |
A | ASN103 |
B | ASP119 |
site_id | AE2 |
Number of Residues | 2 |
Details | binding site for residue RE B 203 |
Chain | Residue |
B | HOH323 |
B | HOH324 |
site_id | AE3 |
Number of Residues | 1 |
Details | binding site for residue RE B 204 |
Chain | Residue |
B | ASP52 |
site_id | AE4 |
Number of Residues | 3 |
Details | binding site for residue CL B 205 |
Chain | Residue |
A | ASN113 |
B | ARG21 |
B | TYR23 |
site_id | AE5 |
Number of Residues | 4 |
Details | binding site for residue CL B 206 |
Chain | Residue |
B | ASN65 |
B | GLY67 |
B | ARG68 |
B | THR69 |
site_id | AE6 |
Number of Residues | 4 |
Details | binding site for residue NA B 207 |
Chain | Residue |
B | SER60 |
B | CYS64 |
B | SER72 |
B | ARG73 |
site_id | AE7 |
Number of Residues | 1 |
Details | binding site for residue RE B 208 |
Chain | Residue |
B | ACT211 |
site_id | AE8 |
Number of Residues | 7 |
Details | binding site for residue RRE B 210 |
Chain | Residue |
A | RE201 |
A | RE202 |
B | ALA11 |
B | HIS15 |
B | ASP87 |
B | ILE88 |
B | THR89 |
site_id | AE9 |
Number of Residues | 7 |
Details | binding site for residue ACT B 211 |
Chain | Residue |
B | GLN57 |
B | ILE58 |
B | ASN59 |
B | TRP63 |
B | ALA107 |
B | TRP108 |
B | RE208 |
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 |