4PRQ
CRYSTAL STRUCTURE OF HEN EGG-WHITE LYSOZYME IN COMPLEX WITH SCLX4 AT 1.72 A RESOLUTION
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 |
| C | 0003796 | molecular_function | lysozyme activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005615 | cellular_component | extracellular space |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005783 | cellular_component | endoplasmic reticulum |
| C | 0016231 | molecular_function | beta-N-acetylglucosaminidase activity |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0016998 | biological_process | cell wall macromolecule catabolic process |
| C | 0031640 | biological_process | killing of cells of another organism |
| C | 0042742 | biological_process | defense response to bacterium |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0050829 | biological_process | defense response to Gram-negative bacterium |
| C | 0050830 | biological_process | defense response to Gram-positive bacterium |
| C | 0051672 | biological_process | obsolete catabolism by organism of cell wall peptidoglycan in other organism |
| D | 0003796 | molecular_function | lysozyme 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 | 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 | 27 |
| Details | BINDING SITE FOR RESIDUE T3Y A 201 |
| Chain | Residue |
| A | CYS6 |
| A | HOH333 |
| A | HOH342 |
| A | HOH347 |
| A | HOH358 |
| B | SER86 |
| B | T3Y202 |
| B | HOH318 |
| B | HOH323 |
| D | LYS1 |
| D | PHE3 |
| A | ASN65 |
| D | GLU7 |
| D | ALA11 |
| D | HIS15 |
| D | SER86 |
| D | ASP87 |
| D | ILE88 |
| D | HOH316 |
| D | HOH335 |
| A | ASN74 |
| A | GLY126 |
| A | CYS127 |
| A | ARG128 |
| A | HOH304 |
| A | HOH310 |
| A | HOH323 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE T3Y A 202 |
| Chain | Residue |
| A | LYS1 |
| A | PHE3 |
| A | ALA11 |
| A | ARG14 |
| A | HIS15 |
| A | SER86 |
| A | ASP87 |
| A | ILE88 |
| A | P6G204 |
| A | HOH309 |
| A | HOH318 |
| A | HOH327 |
| A | HOH344 |
| A | HOH363 |
| A | HOH369 |
| A | HOH399 |
| B | T3Y201 |
| B | HOH329 |
| C | LYS1 |
| C | VAL2 |
| C | HOH311 |
| C | HOH343 |
| D | ASN65 |
| D | ASN74 |
| D | PRO79 |
| D | MG201 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PG4 A 203 |
| Chain | Residue |
| A | TYR20 |
| A | ASN93 |
| A | HOH395 |
| D | TYR20 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE P6G A 204 |
| Chain | Residue |
| A | ARG14 |
| A | T3Y202 |
| D | MG201 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE T3Y B 201 |
| Chain | Residue |
| A | SER86 |
| A | T3Y202 |
| A | HOH322 |
| A | HOH363 |
| B | CYS6 |
| B | ASN65 |
| B | ASN74 |
| B | GLY126 |
| B | CYS127 |
| B | ARG128 |
| B | HOH325 |
| B | HOH329 |
| B | HOH352 |
| B | HOH372 |
| B | HOH384 |
| C | LYS1 |
| C | PHE3 |
| C | GLU7 |
| C | ALA11 |
| C | HIS15 |
| C | SER86 |
| C | ASP87 |
| C | ILE88 |
| C | HOH311 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE T3Y B 202 |
| Chain | Residue |
| B | HOH327 |
| B | HOH338 |
| B | HOH357 |
| C | ASN65 |
| C | ASN74 |
| C | PRO79 |
| C | MG201 |
| D | LYS1 |
| D | VAL2 |
| A | T3Y201 |
| A | HOH304 |
| A | HOH347 |
| B | LYS1 |
| B | PHE3 |
| B | ALA11 |
| B | ARG14 |
| B | HIS15 |
| B | SER86 |
| B | ASP87 |
| B | ILE88 |
| B | PG6206 |
| B | HOH312 |
| B | HOH315 |
| B | HOH318 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE T3Y B 203 |
| Chain | Residue |
| B | ARG61 |
| B | TRP62 |
| B | GLY102 |
| B | ASN103 |
| B | GLY104 |
| B | ASN106 |
| B | PG4204 |
| B | MG207 |
| B | HOH332 |
| B | HOH333 |
| B | HOH346 |
| B | HOH348 |
| B | HOH358 |
| B | HOH368 |
| B | HOH370 |
| B | HOH387 |
| B | HOH390 |
| B | HOH394 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PG4 B 204 |
| Chain | Residue |
| B | TRP62 |
| B | T3Y203 |
| B | MG207 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PG4 B 205 |
| Chain | Residue |
| B | ARG68 |
| B | PRO70 |
| B | ALA122 |
| B | TRP123 |
| B | HOH383 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PG6 B 206 |
| Chain | Residue |
| B | ARG14 |
| B | T3Y202 |
| C | MG201 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 207 |
| Chain | Residue |
| B | T3Y203 |
| B | PG4204 |
| B | HOH394 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG C 201 |
| Chain | Residue |
| B | T3Y202 |
| B | PG6206 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG D 201 |
| Chain | Residue |
| A | T3Y202 |
| A | P6G204 |
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 | 8 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | GLU35 | |
| A | ASP52 | |
| B | GLU35 | |
| B | ASP52 | |
| C | GLU35 | |
| C | ASP52 | |
| D | GLU35 | |
| D | ASP52 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP101 | |
| B | ASP101 | |
| C | ASP101 | |
| D | 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 |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 203 |
| Chain | Residue | Details |
| C | GLU35 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | ASN46 | |
| C | ASP48 | |
| C | SER50 | |
| C | ASP52 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction |
| C | ASN59 |
| site_id | MCSA4 |
| 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 |
