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	0004519	molecular_function	endonuclease activity
A	0004521	molecular_function	RNA endonuclease activity
A	0004540	molecular_function	RNA nuclease activity
A	0008150	biological_process	biological_process
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	0004519	molecular_function	endonuclease activity
B	0004521	molecular_function	RNA endonuclease activity
B	0004540	molecular_function	RNA nuclease activity
B	0008150	biological_process	biological_process
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	0004519	molecular_function	endonuclease activity
C	0004521	molecular_function	RNA endonuclease activity
C	0004540	molecular_function	RNA nuclease activity
C	0008150	biological_process	biological_process
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	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:2844811

Chain	Residue	Details
A	HIS40
B	HIS40
C	HIS40

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:2844811

Chain	Residue	Details
A	GLU58
B	GLU58
C	GLU58

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	ACT_SITE: Proton donor

Chain	Residue	Details
A	HIS92
B	HIS92
C	HIS92

---

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

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