3FI5

Crystal Structure of T4 Lysozyme Mutant R96W

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme activity
A	0003824	molecular_function	catalytic activity
A	0009253	biological_process	peptidoglycan catabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0016998	biological_process	cell wall macromolecule catabolic process
A	0030430	cellular_component	host cell cytoplasm
A	0031640	biological_process	killing of cells of another organism
A	0042742	biological_process	defense response to bacterium
A	0044659	biological_process	viral release from host cell by cytolysis
B	0003796	molecular_function	lysozyme activity
B	0003824	molecular_function	catalytic activity
B	0009253	biological_process	peptidoglycan catabolic process
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	0030430	cellular_component	host cell cytoplasm
B	0031640	biological_process	killing of cells of another organism
B	0042742	biological_process	defense response to bacterium
B	0044659	biological_process	viral release from host cell by cytolysis
C	0003796	molecular_function	lysozyme activity
C	0003824	molecular_function	catalytic activity
C	0009253	biological_process	peptidoglycan catabolic process
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0016998	biological_process	cell wall macromolecule catabolic process
C	0030430	cellular_component	host cell cytoplasm
C	0031640	biological_process	killing of cells of another organism
C	0042742	biological_process	defense response to bacterium
C	0044659	biological_process	viral release from host cell by cytolysis
D	0003796	molecular_function	lysozyme activity
D	0003824	molecular_function	catalytic activity
D	0009253	biological_process	peptidoglycan catabolic process
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	0030430	cellular_component	host cell cytoplasm
D	0031640	biological_process	killing of cells of another organism
D	0042742	biological_process	defense response to bacterium
D	0044659	biological_process	viral release from host cell by cytolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 502

Chain	Residue
A	ALA93

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA A 513

Chain	Residue
A	GLU11
A	ARG14
A	TYR18
A	HOH1429

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE IPA A 601

Chain	Residue
A	HOH1449
A	HOH1691
A	HOH1839
A	HOH2330
A	ARG125
A	TRP126
A	ASP127
A	GLU128

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL B 506

Chain	Residue
B	THR142
B	ASN144
B	ARG145
B	HOH1203
B	HOH1698
B	HOH2021

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NA B 512

Chain	Residue
B	GLU11
B	HOH1226

---

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL C 503

Chain	Residue
C	ASN144

---

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA C 511

Chain	Residue
C	GLU11
C	HOH1447
C	HOH1692

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1892846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 206l

Chain	Residue	Details
A	GLU11
A	ASP20

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 206l

Chain	Residue	Details
B	GLU11
B	ASP20

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 206l

Chain	Residue	Details
C	GLU11
C	ASP20

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 206l

Chain	Residue	Details
D	GLU11
D	ASP20

---

site_id	MCSA1
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
A	GLU11	proton shuttle (general acid/base)
A	ASP20	covalent catalysis

---

site_id	MCSA2
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
B	GLU11	proton shuttle (general acid/base)
B	ASP20	covalent catalysis

---

site_id	MCSA3
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
C	GLU11	proton shuttle (general acid/base)
C	ASP20	covalent catalysis

---

site_id	MCSA4
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
D	GLU11	proton shuttle (general acid/base)
D	ASP20	covalent catalysis

---