1DFJ

RIBONUCLEASE INHIBITOR COMPLEXED WITH RIBONUCLEASE A

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0003676	molecular_function	nucleic acid binding
E	0004518	molecular_function	nuclease activity
E	0004519	molecular_function	endonuclease activity
E	0004522	molecular_function	ribonuclease A activity
E	0004540	molecular_function	RNA nuclease activity
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0016787	molecular_function	hydrolase activity
E	0016829	molecular_function	lyase activity
E	0050830	biological_process	defense response to Gram-positive bacterium
I	0005654	cellular_component	nucleoplasm
I	0005737	cellular_component	cytoplasm
I	0005886	cellular_component	plasma membrane
I	0008428	molecular_function	ribonuclease inhibitor activity
I	0016477	biological_process	cell migration
I	0030027	cellular_component	lamellipodium
I	0032311	cellular_component	angiogenin-PRI complex
I	0034315	biological_process	regulation of Arp2/3 complex-mediated actin nucleation
I	0045765	biological_process	regulation of angiogenesis
I	0050727	biological_process	regulation of inflammatory response

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 E 1001

Chain	Residue
E	GLN11
E	HIS12
E	LYS41
E	HIS119
E	PHE120
I	ASP431

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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
E	CYS40-PHE46

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: N-acetylmethionine => ECO:0000269|PubMed:3219361

Chain	Residue	Details
I	MET1

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P13489

Chain	Residue	Details
I	SER86

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site_id	SWS_FT_FI3
Number of Residues	5
Details	BINDING:

Chain	Residue	Details
E	LYS7
E	ARG10
E	LYS41
E	LYS66
E	ARG85

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site_id	SWS_FT_FI4
Number of Residues	4
Details	CARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761

Chain	Residue	Details
E	LYS1
E	LYS7
E	LYS37
E	LYS41

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site_id	SWS_FT_FI5
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:19358553

Chain	Residue	Details
E	ASN34

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 164

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

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