3RID
X-ray structure of the C-terminal swapped dimer of P114A variant of Ribonuclease A
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 | 0003676 | molecular_function | nucleic acid binding |
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 | 0016829 | molecular_function | lyase activity |
B | 0050830 | biological_process | defense response to Gram-positive bacterium |
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 | 0003676 | molecular_function | nucleic acid binding |
D | 0004519 | molecular_function | endonuclease activity |
D | 0004522 | molecular_function | ribonuclease A activity |
D | 0004540 | molecular_function | RNA nuclease activity |
D | 0005515 | molecular_function | protein binding |
D | 0005576 | cellular_component | extracellular region |
D | 0016829 | molecular_function | lyase activity |
D | 0050830 | biological_process | defense response to Gram-positive bacterium |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE CGP A 751 |
Chain | Residue |
A | HIS12 |
A | HOH1785 |
A | HOH1797 |
A | HOH1870 |
B | PHE120 |
B | ASP121 |
B | PO4801 |
B | HOH1360 |
A | VAL43 |
A | ASN44 |
A | THR45 |
A | ARG85 |
A | GLU86 |
A | HOH1603 |
A | HOH1621 |
A | HOH1730 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 B 801 |
Chain | Residue |
A | GLN11 |
A | HIS12 |
A | LYS41 |
A | CGP751 |
A | HOH1327 |
B | HIS119 |
B | PHE120 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 B 802 |
Chain | Residue |
A | HIS119 |
A | PHE120 |
B | GLN11 |
B | HIS12 |
B | LYS41 |
B | CGP753 |
B | HOH1397 |
B | HOH1447 |
B | HOH1618 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE CGP B 753 |
Chain | Residue |
A | PHE120 |
A | ASP121 |
B | HIS12 |
B | VAL43 |
B | ASN44 |
B | THR45 |
B | LYS66 |
B | ARG85 |
B | GLU86 |
B | PO4802 |
B | HOH1401 |
B | HOH1422 |
B | HOH1423 |
B | HOH1424 |
B | HOH1559 |
B | HOH1747 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 C 803 |
Chain | Residue |
C | GLN11 |
C | HIS12 |
C | LYS41 |
C | CGP755 |
C | HOH1535 |
D | HIS119 |
D | PHE120 |
site_id | AC6 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE CGP C 755 |
Chain | Residue |
C | HIS12 |
C | VAL43 |
C | ASN44 |
C | THR45 |
C | ARG85 |
C | GLU86 |
C | PO4803 |
C | HOH1507 |
C | HOH1767 |
C | HOH1780 |
C | HOH1912 |
D | PHE120 |
D | ASP121 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 D 804 |
Chain | Residue |
C | HIS119 |
C | PHE120 |
D | GLN11 |
D | HIS12 |
D | LYS41 |
D | CGP757 |
D | HOH1472 |
D | HOH1776 |
site_id | AC8 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE CGP D 757 |
Chain | Residue |
C | PHE120 |
C | ASP121 |
C | ALA122 |
C | HOH1503 |
D | HIS12 |
D | VAL43 |
D | ASN44 |
D | THR45 |
D | LYS66 |
D | ARG85 |
D | GLU86 |
D | PO4804 |
D | HOH1500 |
D | HOH1502 |
D | HOH1517 |
D | HOH1524 |
D | HOH1571 |
D | HOH1722 |
D | HOH1916 |
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 | 4 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | HIS12 | |
B | HIS12 | |
C | HIS12 | |
D | HIS12 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | HIS119 | |
B | HIS119 | |
C | HIS119 | |
D | HIS119 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS7 | |
B | ARG85 | |
C | LYS7 | |
C | ARG10 | |
C | LYS41 | |
C | LYS66 | |
C | ARG85 | |
D | LYS7 | |
D | ARG10 | |
D | LYS41 | |
D | LYS66 | |
A | ARG10 | |
D | ARG85 | |
A | LYS41 | |
A | LYS66 | |
A | ARG85 | |
B | LYS7 | |
B | ARG10 | |
B | LYS41 | |
B | LYS66 |
site_id | SWS_FT_FI4 |
Number of Residues | 16 |
Details | CARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761 |
Chain | Residue | Details |
A | LYS1 | |
C | LYS7 | |
C | LYS37 | |
C | LYS41 | |
D | LYS1 | |
D | LYS7 | |
D | LYS37 | |
D | LYS41 | |
A | LYS7 | |
A | LYS37 | |
A | LYS41 | |
B | LYS1 | |
B | LYS7 | |
B | LYS37 | |
B | LYS41 | |
C | LYS1 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:19358553 |
Chain | Residue | Details |
A | ASN34 | |
B | ASN34 | |
C | ASN34 | |
D | ASN34 |
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 |
site_id | MCSA3 |
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 |
site_id | MCSA4 |
Number of Residues | 5 |
Details | M-CSA 164 |
Chain | Residue | Details |
D | HIS12 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
D | LYS41 | electrostatic stabiliser, hydrogen bond donor |
D | HIS119 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
D | PHE120 | electrostatic stabiliser, hydrogen bond donor |
D | ASP121 | electrostatic stabiliser, hydrogen bond acceptor |