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 |