5E5F

X-ray structure of the complex between RNase A and compound 4-PF6 ([(PPh3)Au(mi-pbi)Pt(Me)(DMSO)][PF6]), the heterobimetallic derivative obtained in the reaction between the organometallic compound [Pt(pbi)(Me)(DMSO)], pbi=2-(2'-pyridil)benzimidazole (compound 3) and the gold(I) compound [Au(Ph3P)][PF6]

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue AU A 201

Chain	Residue
A	HIS105
A	HOH400
A	HOH409
A	HOH410

---

site_id	AC2
Number of Residues	7
Details	binding site for residue SO4 A 202

Chain	Residue
A	HOH304
A	HOH363
A	GLN11
A	HIS12
A	LYS41
A	HIS119
A	PHE120

---

site_id	AC3
Number of Residues	5
Details	binding site for residue ACT A 203

Chain	Residue
A	HIS12
A	ASN44
A	THR45
A	PHE120
A	HOH407

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton donor"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	8
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	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; partial","featureId":"CAR_000006","evidences":[{"source":"PubMed","id":"19358553","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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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

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