2I26
Crystal structure analysis of the nurse shark new antigen receptor ancestral variable domain in complex with lysozyme
Functional Information from GO Data
Chain | GOid | namespace | contents |
L | 0003796 | molecular_function | lysozyme activity |
L | 0005515 | molecular_function | protein binding |
L | 0005576 | cellular_component | extracellular region |
L | 0005615 | cellular_component | extracellular space |
L | 0005737 | cellular_component | cytoplasm |
L | 0005783 | cellular_component | endoplasmic reticulum |
L | 0016231 | molecular_function | beta-N-acetylglucosaminidase activity |
L | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
L | 0016998 | biological_process | cell wall macromolecule catabolic process |
L | 0031640 | biological_process | killing of cells of another organism |
L | 0042742 | biological_process | defense response to bacterium |
L | 0042802 | molecular_function | identical protein binding |
L | 0050829 | biological_process | defense response to Gram-negative bacterium |
L | 0050830 | biological_process | defense response to Gram-positive bacterium |
L | 0051672 | biological_process | obsolete catabolism by organism of cell wall peptidoglycan in other organism |
M | 0003796 | molecular_function | lysozyme activity |
M | 0005515 | molecular_function | protein binding |
M | 0005576 | cellular_component | extracellular region |
M | 0005615 | cellular_component | extracellular space |
M | 0005737 | cellular_component | cytoplasm |
M | 0005783 | cellular_component | endoplasmic reticulum |
M | 0016231 | molecular_function | beta-N-acetylglucosaminidase activity |
M | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
M | 0016998 | biological_process | cell wall macromolecule catabolic process |
M | 0031640 | biological_process | killing of cells of another organism |
M | 0042742 | biological_process | defense response to bacterium |
M | 0042802 | molecular_function | identical protein binding |
M | 0050829 | biological_process | defense response to Gram-negative bacterium |
M | 0050830 | biological_process | defense response to Gram-positive bacterium |
M | 0051672 | biological_process | obsolete catabolism by organism of cell wall peptidoglycan in other organism |
Q | 0003796 | molecular_function | lysozyme activity |
Q | 0005515 | molecular_function | protein binding |
Q | 0005576 | cellular_component | extracellular region |
Q | 0005615 | cellular_component | extracellular space |
Q | 0005737 | cellular_component | cytoplasm |
Q | 0005783 | cellular_component | endoplasmic reticulum |
Q | 0016231 | molecular_function | beta-N-acetylglucosaminidase activity |
Q | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
Q | 0016998 | biological_process | cell wall macromolecule catabolic process |
Q | 0031640 | biological_process | killing of cells of another organism |
Q | 0042742 | biological_process | defense response to bacterium |
Q | 0042802 | molecular_function | identical protein binding |
Q | 0050829 | biological_process | defense response to Gram-negative bacterium |
Q | 0050830 | biological_process | defense response to Gram-positive bacterium |
Q | 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 | 5 |
Details | BINDING SITE FOR RESIDUE SO4 L 201 |
Chain | Residue |
L | ARG125 |
L | GLY126 |
L | CYS127 |
L | ARG128 |
P | THR11 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 M 202 |
Chain | Residue |
M | ARG125 |
M | GLY126 |
M | ARG128 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 Q 203 |
Chain | Residue |
Q | GLY126 |
Q | CYS127 |
Q | ARG128 |
Q | ARG125 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 Q 204 |
Chain | Residue |
M | ARG73 |
Q | ARG14 |
Q | HIS15 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 M 205 |
Chain | Residue |
M | ALA11 |
M | ARG14 |
M | HIS15 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 Q 206 |
Chain | Residue |
M | TYR20 |
Q | ARG125 |
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 |
L | CYS76-CYS94 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: |
Chain | Residue | Details |
L | GLU35 | |
L | ASP52 | |
M | GLU35 | |
M | ASP52 | |
Q | GLU35 | |
Q | ASP52 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
L | ASP101 | |
M | ASP101 | |
Q | ASP101 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 132l |
Chain | Residue | Details |
L | GLU35 | |
L | ASP52 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 132l |
Chain | Residue | Details |
M | GLU35 | |
M | ASP52 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 132l |
Chain | Residue | Details |
Q | GLU35 | |
Q | ASP52 |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 203 |
Chain | Residue | Details |
L | GLU35 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
L | ASN46 | |
L | ASP48 | |
L | SER50 | |
L | ASP52 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction |
L | ASN59 |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 203 |
Chain | Residue | Details |
M | GLU35 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
M | ASN46 | |
M | ASP48 | |
M | SER50 | |
M | ASP52 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction |
M | ASN59 |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 203 |
Chain | Residue | Details |
Q | GLU35 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
Q | ASN46 | |
Q | ASP48 | |
Q | SER50 | |
Q | ASP52 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction |
Q | ASN59 |