5ET4

Structure of RNase A-K7H/R10H in complex with 3'-CMP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003676	molecular_function	nucleic acid binding
A	0004518	molecular_function	nuclease activity
A	0004519	molecular_function	endonuclease activity
A	0004522	molecular_function	ribonuclease A activity
A	0004540	molecular_function	RNA nuclease activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0016787	molecular_function	hydrolase activity
A	0016829	molecular_function	lyase activity
A	0050830	biological_process	defense response to Gram-positive bacterium
B	0003676	molecular_function	nucleic acid binding
B	0004518	molecular_function	nuclease activity
B	0004519	molecular_function	endonuclease activity
B	0004522	molecular_function	ribonuclease A activity
B	0004540	molecular_function	RNA nuclease activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0016787	molecular_function	hydrolase activity
B	0016829	molecular_function	lyase activity
B	0050830	biological_process	defense response to Gram-positive bacterium
C	0003676	molecular_function	nucleic acid binding
C	0004518	molecular_function	nuclease activity
C	0004519	molecular_function	endonuclease activity
C	0004522	molecular_function	ribonuclease A activity
C	0004540	molecular_function	RNA nuclease activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0016787	molecular_function	hydrolase activity
C	0016829	molecular_function	lyase activity
C	0050830	biological_process	defense response to Gram-positive bacterium
D	0003676	molecular_function	nucleic acid binding
D	0004518	molecular_function	nuclease activity
D	0004519	molecular_function	endonuclease activity
D	0004522	molecular_function	ribonuclease A activity
D	0004540	molecular_function	RNA nuclease activity
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0016787	molecular_function	hydrolase activity
D	0016829	molecular_function	lyase activity
D	0050830	biological_process	defense response to Gram-positive bacterium

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue C3P A 500

Chain	Residue
A	GLN11
A	HOH604
A	HOH607
A	HOH629
A	HOH630
A	HOH642
B	HOH636
A	HIS12
A	LYS41
A	VAL43
A	ASN44
A	THR45
A	LYS66
A	HIS119
A	PHE120

---

site_id	AC2
Number of Residues	11
Details	binding site for residue C3P B 500

Chain	Residue
B	GLN11
B	HIS12
B	LYS41
B	VAL43
B	ASN44
B	THR45
B	HIS119
B	PHE120
B	HOH601
B	HOH606
B	HOH667

---

site_id	AC3
Number of Residues	11
Details	binding site for residue C3P C 201

Chain	Residue
C	GLN11
C	HIS12
C	LYS41
C	VAL43
C	ASN44
C	THR45
C	HIS119
C	PHE120
C	ASP121
C	HOH343
C	HOH360

---

site_id	AC4
Number of Residues	5
Details	binding site for residue MPD C 202

Chain	Residue
C	THR99
C	THR100
C	GLN101
D	SER15
D	SER50

---

site_id	AC5
Number of Residues	11
Details	binding site for residue C3P D 400

Chain	Residue
D	HIS7
D	GLN11
D	HIS12
D	LYS41
D	VAL43
D	ASN44
D	THR45
D	HIS119
D	PHE120
D	HOH553
D	HOH556

---

Functional Information from PROSITE/UniProt

site_id	PS00127
Number of Residues	7
Details	RNASE_PANCREATIC Pancreatic ribonuclease family signature. CKpvNTF

Chain	Residue	Details
A	CYS40-PHE46

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	32
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	16
Details	Glycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"4030761","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; partial","featureId":"CAR_000006","evidences":[{"source":"PubMed","id":"19358553","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 164

Chain	Residue	Details
A	HIS12	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	LYS41	electrostatic stabiliser, hydrogen bond donor
A	HIS119	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	PHE120	electrostatic stabiliser, hydrogen bond donor
A	ASP121	electrostatic stabiliser, hydrogen bond acceptor

---

site_id	MCSA2
Number of Residues	5
Details	M-CSA 164

Chain	Residue	Details
B	HIS12	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	LYS41	electrostatic stabiliser, hydrogen bond donor
B	HIS119	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	PHE120	electrostatic stabiliser, hydrogen bond donor
B	ASP121	electrostatic stabiliser, hydrogen bond acceptor

---

site_id	MCSA3
Number of Residues	5
Details	M-CSA 164

Chain	Residue	Details
C	HIS12	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	LYS41	electrostatic stabiliser, hydrogen bond donor
C	HIS119	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	PHE120	electrostatic stabiliser, hydrogen bond donor
C	ASP121	electrostatic stabiliser, hydrogen bond acceptor

---

site_id	MCSA4
Number of Residues	5
Details	M-CSA 164

Chain	Residue	Details
D	HIS12	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	LYS41	electrostatic stabiliser, hydrogen bond donor
D	HIS119	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	PHE120	electrostatic stabiliser, hydrogen bond donor
D	ASP121	electrostatic stabiliser, hydrogen bond acceptor

---