1RN1

THREE-DIMENSIONAL STRUCTURE OF GLN 25-RIBONUCLEASE T1 AT 1.84 ANGSTROMS RESOLUTION: STRUCTURAL VARIATIONS AT THE BASE RECOGNITION AND CATALYTIC SITES

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001411	cellular_component	hyphal tip
A	0003723	molecular_function	RNA binding
A	0004518	molecular_function	nuclease activity
A	0004519	molecular_function	endonuclease activity
A	0004521	molecular_function	RNA endonuclease activity
A	0004540	molecular_function	RNA nuclease activity
A	0016787	molecular_function	hydrolase activity
A	0016829	molecular_function	lyase activity
A	0030428	cellular_component	cell septum
A	0046589	molecular_function	ribonuclease T1 activity
B	0001411	cellular_component	hyphal tip
B	0003723	molecular_function	RNA binding
B	0004518	molecular_function	nuclease activity
B	0004519	molecular_function	endonuclease activity
B	0004521	molecular_function	RNA endonuclease activity
B	0004540	molecular_function	RNA nuclease activity
B	0016787	molecular_function	hydrolase activity
B	0016829	molecular_function	lyase activity
B	0030428	cellular_component	cell septum
B	0046589	molecular_function	ribonuclease T1 activity
C	0001411	cellular_component	hyphal tip
C	0003723	molecular_function	RNA binding
C	0004518	molecular_function	nuclease activity
C	0004519	molecular_function	endonuclease activity
C	0004521	molecular_function	RNA endonuclease activity
C	0004540	molecular_function	RNA nuclease activity
C	0016787	molecular_function	hydrolase activity
C	0016829	molecular_function	lyase activity
C	0030428	cellular_component	cell septum
C	0046589	molecular_function	ribonuclease T1 activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 105

Chain	Residue
A	TYR38
A	HIS40
A	GLU58
A	ARG77
A	HIS92

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 106

Chain	Residue
B	ARG77
B	HIS92
B	PHE100
B	ASN36
B	TYR38
B	HIS40
B	GLU58

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 C 107

Chain	Residue
C	TYR38
C	HIS40
C	GLU58
C	ARG77
C	HIS92
C	ASN98
C	PHE100
C	HOH150

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Active site: {"evidences":[{"source":"PubMed","id":"2844811","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"2844811","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Active site: {"description":"Proton donor"}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1b2m

Chain	Residue	Details
A	GLU58
A	HIS40
A	HIS92

---

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1b2m

Chain	Residue	Details
B	GLU58
B	HIS40
B	HIS92

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1b2m

Chain	Residue	Details
C	GLU58
C	HIS40
C	HIS92

---

site_id	MCSA1
Number of Residues	6
Details	M-CSA 414

Chain	Residue	Details
A	TYR38	electrostatic stabiliser
A	HIS40	proton shuttle (general acid/base)
A	GLU58	proton shuttle (general acid/base)
A	ARG77	electrostatic stabiliser
A	HIS92	proton shuttle (general acid/base)
A	PHE100	electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	6
Details	M-CSA 414

Chain	Residue	Details
B	TYR38	electrostatic stabiliser
B	HIS40	proton shuttle (general acid/base)
B	GLU58	proton shuttle (general acid/base)
B	ARG77	electrostatic stabiliser
B	HIS92	proton shuttle (general acid/base)
B	PHE100	electrostatic stabiliser

---

site_id	MCSA3
Number of Residues	6
Details	M-CSA 414

Chain	Residue	Details
C	TYR38	electrostatic stabiliser
C	HIS40	proton shuttle (general acid/base)
C	GLU58	proton shuttle (general acid/base)
C	ARG77	electrostatic stabiliser
C	HIS92	proton shuttle (general acid/base)
C	PHE100	electrostatic stabiliser

---