1RNM

RIBONUCLEASE A COMPLEX WITH CYTIDYLIC ACID (5'CMP) CRYSTALLIZED FROM 80% AMMONIUM SULPHATE

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 E 125

Chain	Residue
E	GLN11
E	HIS12
E	LYS41
E	VAL118
E	HIS119
E	PHE120
E	C5P200
E	HOH219
E	HOH272

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 E 126

Chain	Residue
E	SER23
E	HOH217
E	HOH246
E	HOH260

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 E 127

Chain	Residue
E	LYS66
E	LYS66
E	ALA122
E	ALA122
E	SER123
E	SER123
E	C5P200
E	C5P200
E	HOH253
E	HOH253

---

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE C5P E 200

Chain	Residue
E	HIS12
E	LYS41
E	VAL43
E	ASN44
E	THR45
E	LYS66
E	PHE120
E	SO4125
E	SO4127
E	SO4127
E	HOH247

---

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
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	1
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	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1rbn

Chain	Residue	Details
E	PHE120
E	HIS119
E	HIS12
E	LYS41

---

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1rbn

Chain	Residue	Details
E	HIS119
E	HIS12
E	LYS41

---

site_id	MCSA1
Number of Residues	5
Details	M-CSA 164

Chain

Residue

Details

---