4PEQ

Structure of bovine ribonuclease inhibitor complexed with bovine ribonuclease I

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003676	molecular_function	nucleic acid binding
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	0016829	molecular_function	lyase activity
A	0050830	biological_process	defense response to Gram-positive bacterium
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005886	cellular_component	plasma membrane
B	0008428	molecular_function	ribonuclease inhibitor activity
B	0016477	biological_process	cell migration
B	0030027	cellular_component	lamellipodium
B	0032311	cellular_component	angiogenin-PRI complex
B	0034315	biological_process	regulation of Arp2/3 complex-mediated actin nucleation
B	0045765	biological_process	regulation of angiogenesis
C	0003676	molecular_function	nucleic acid binding
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	0016829	molecular_function	lyase activity
C	0050830	biological_process	defense response to Gram-positive bacterium
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0005886	cellular_component	plasma membrane
D	0008428	molecular_function	ribonuclease inhibitor activity
D	0016477	biological_process	cell migration
D	0030027	cellular_component	lamellipodium
D	0032311	cellular_component	angiogenin-PRI complex
D	0034315	biological_process	regulation of Arp2/3 complex-mediated actin nucleation
D	0045765	biological_process	regulation of angiogenesis

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	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	HIS12
C	HIS12

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor

Chain	Residue	Details
A	HIS119
C	HIS119

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site_id	SWS_FT_FI3
Number of Residues	10
Details	BINDING:

Chain	Residue	Details
A	LYS7
C	ARG85
A	ARG10
A	LYS41
A	LYS66
A	ARG85
C	LYS7
C	ARG10
C	LYS41
C	LYS66

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site_id	SWS_FT_FI4
Number of Residues	8
Details	CARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761

Chain	Residue	Details
A	LYS1
A	LYS7
A	LYS37
A	LYS41
C	LYS1
C	LYS7
C	LYS37
C	LYS41

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site_id	SWS_FT_FI5
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:19358553

Chain	Residue	Details
A	ASN34
C	ASN34

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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

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site_id	MCSA2
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

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