5JEN
Crystal structure of the anti-sigma factor RsiV bound to lysozyme
Functional Information from GO Data
Chain | GOid | namespace | contents |
B | 0003796 | molecular_function | lysozyme activity |
B | 0003824 | molecular_function | catalytic 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 | 0016787 | molecular_function | hydrolase 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 |
D | 0003796 | molecular_function | lysozyme activity |
D | 0003824 | molecular_function | catalytic activity |
D | 0005515 | molecular_function | protein binding |
D | 0005576 | cellular_component | extracellular region |
D | 0005615 | cellular_component | extracellular space |
D | 0005737 | cellular_component | cytoplasm |
D | 0005783 | cellular_component | endoplasmic reticulum |
D | 0016231 | molecular_function | beta-N-acetylglucosaminidase activity |
D | 0016787 | molecular_function | hydrolase activity |
D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
D | 0016998 | biological_process | cell wall macromolecule catabolic process |
D | 0031640 | biological_process | killing of cells of another organism |
D | 0042742 | biological_process | defense response to bacterium |
D | 0042802 | molecular_function | identical protein binding |
D | 0050829 | biological_process | defense response to Gram-negative bacterium |
D | 0050830 | biological_process | defense response to Gram-positive bacterium |
D | 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 | 6 |
Details | binding site for residue NA A 400 |
Chain | Residue |
A | THR239 |
A | HOH506 |
A | HOH538 |
A | HOH571 |
A | HOH584 |
A | HOH607 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue NA A 401 |
Chain | Residue |
A | HOH504 |
B | ASP52 |
B | HOH311 |
A | SER168 |
A | SER169 |
A | TYR255 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue NA B 200 |
Chain | Residue |
B | SER60 |
B | CYS64 |
B | ASN65 |
B | SER72 |
B | ARG73 |
B | HOH318 |
B | HOH341 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue CL B 201 |
Chain | Residue |
A | LYS232 |
B | GLY67 |
B | ARG68 |
B | THR69 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue NA C 400 |
Chain | Residue |
C | THR239 |
C | HOH545 |
C | HOH583 |
C | HOH586 |
C | HOH613 |
C | HOH615 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue NA C 401 |
Chain | Residue |
C | SER168 |
C | SER169 |
C | TYR255 |
C | HOH507 |
D | ASP52 |
D | HOH336 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue NA D 200 |
Chain | Residue |
D | SER60 |
D | CYS64 |
D | SER72 |
D | ARG73 |
D | HOH337 |
D | HOH344 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue CL D 201 |
Chain | Residue |
C | LYS232 |
D | ASN65 |
D | GLY67 |
D | ARG68 |
D | THR69 |
D | SER72 |
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 |
B | CYS76-CYS94 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 256 |
Details | Domain: {"description":"C-type lysozyme","evidences":[{"source":"PROSITE-ProRule","id":"PRU00680","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | Active site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Binding site: {} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | MCSA1 |
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 |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 203 |
Chain | Residue | Details |
D | GLU35 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
D | ASN46 | |
D | ASP48 | |
D | SER50 | |
D | ASP52 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction |
D | ASN59 |