2P4A

X-ray structure of a camelid affinity matured single-domain vhh antibody fragment in complex with RNASE A

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	0002250	biological_process	adaptive immune response
B	0002376	biological_process	immune system process
B	0005576	cellular_component	extracellular region
B	0019814	cellular_component	immunoglobulin complex
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	0002250	biological_process	adaptive immune response
D	0002376	biological_process	immune system process
D	0005576	cellular_component	extracellular region
D	0019814	cellular_component	immunoglobulin complex

Functional Information from PDB Data

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	2
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

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

Chain

Residue

Details

Chain

Residue

Details

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

Catalytic Information from CSA

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

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1rbn

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1rbn

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1rbn

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

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