Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4M6D

Crystal structure of the aptamer minF-lysozyme complex.

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
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
E	0003796	molecular_function	lysozyme activity
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0005615	cellular_component	extracellular space
E	0005737	cellular_component	cytoplasm
E	0005783	cellular_component	endoplasmic reticulum
E	0016231	molecular_function	beta-N-acetylglucosaminidase activity
E	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
E	0016998	biological_process	cell wall macromolecule catabolic process
E	0031640	biological_process	killing of cells of another organism
E	0042742	biological_process	defense response to bacterium
E	0042802	molecular_function	identical protein binding
E	0050829	biological_process	defense response to Gram-negative bacterium
E	0050830	biological_process	defense response to Gram-positive bacterium
E	0051672	biological_process	obsolete catabolism by organism of cell wall peptidoglycan in other organism
G	0003796	molecular_function	lysozyme activity
G	0005515	molecular_function	protein binding
G	0005576	cellular_component	extracellular region
G	0005615	cellular_component	extracellular space
G	0005737	cellular_component	cytoplasm
G	0005783	cellular_component	endoplasmic reticulum
G	0016231	molecular_function	beta-N-acetylglucosaminidase activity
G	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
G	0016998	biological_process	cell wall macromolecule catabolic process
G	0031640	biological_process	killing of cells of another organism
G	0042742	biological_process	defense response to bacterium
G	0042802	molecular_function	identical protein binding
G	0050829	biological_process	defense response to Gram-negative bacterium
G	0050830	biological_process	defense response to Gram-positive bacterium
G	0051672	biological_process	obsolete catabolism by organism of cell wall peptidoglycan in other organism
I	0003796	molecular_function	lysozyme activity
I	0005515	molecular_function	protein binding
I	0005576	cellular_component	extracellular region
I	0005615	cellular_component	extracellular space
I	0005737	cellular_component	cytoplasm
I	0005783	cellular_component	endoplasmic reticulum
I	0016231	molecular_function	beta-N-acetylglucosaminidase activity
I	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
I	0016998	biological_process	cell wall macromolecule catabolic process
I	0031640	biological_process	killing of cells of another organism
I	0042742	biological_process	defense response to bacterium
I	0042802	molecular_function	identical protein binding
I	0050829	biological_process	defense response to Gram-negative bacterium
I	0050830	biological_process	defense response to Gram-positive bacterium
I	0051672	biological_process	obsolete catabolism by organism of cell wall peptidoglycan in other organism
K	0003796	molecular_function	lysozyme activity
K	0005515	molecular_function	protein binding
K	0005576	cellular_component	extracellular region
K	0005615	cellular_component	extracellular space
K	0005737	cellular_component	cytoplasm
K	0005783	cellular_component	endoplasmic reticulum
K	0016231	molecular_function	beta-N-acetylglucosaminidase activity
K	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
K	0016998	biological_process	cell wall macromolecule catabolic process
K	0031640	biological_process	killing of cells of another organism
K	0042742	biological_process	defense response to bacterium
K	0042802	molecular_function	identical protein binding
K	0050829	biological_process	defense response to Gram-negative bacterium
K	0050830	biological_process	defense response to Gram-positive bacterium
K	0051672	biological_process	obsolete catabolism by organism of cell wall peptidoglycan in other organism

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	12
Details	ACT_SITE:

Chain	Residue	Details
A	GLU35
I	ASP52
K	GLU35
K	ASP52
A	ASP52
C	GLU35
C	ASP52
E	GLU35
E	ASP52
G	GLU35
G	ASP52
I	GLU35

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING:

Chain	Residue	Details
A	ASP101
C	ASP101
E	ASP101
G	ASP101
I	ASP101
K	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
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	MCSA3
Number of Residues	6
Details	M-CSA 203

Chain	Residue	Details
E	GLU35	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	ASN46
E	ASP48
E	SER50
E	ASP52	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction
E	ASN59

site_id	MCSA4
Number of Residues	6
Details	M-CSA 203

Chain	Residue	Details
G	GLU35	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
G	ASN46
G	ASP48
G	SER50
G	ASP52	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction
G	ASN59

site_id	MCSA5
Number of Residues	6
Details	M-CSA 203

Chain	Residue	Details
I	GLU35	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
I	ASN46
I	ASP48
I	SER50
I	ASP52	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction
I	ASN59

site_id	MCSA6
Number of Residues	6
Details	M-CSA 203

Chain	Residue	Details
K	GLU35	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
K	ASN46
K	ASP48
K	SER50
K	ASP52	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction
K	ASN59

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)