1RNN
RIBONUCLEASE A COMPLEX WITH CYTIDYLIC ACID (5'CMP) CRYSTALLIZED FROM 8M SODIUM FORMATE
Functional Information from GO Data
Chain | GOid | namespace | contents |
E | 0003676 | molecular_function | nucleic acid binding |
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 | 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 | 10 |
Details | BINDING SITE FOR RESIDUE C5P E 200 |
Chain | Residue |
E | HIS12 |
E | HOH262 |
E | LYS41 |
E | VAL43 |
E | ASN44 |
E | THR45 |
E | HIS119 |
E | PHE120 |
E | FMT131 |
E | HOH255 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT E 131 |
Chain | Residue |
E | GLN11 |
E | HIS12 |
E | HIS119 |
E | PHE120 |
E | C5P200 |
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 | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
E | HIS12 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
E | HIS119 |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | BINDING: |
Chain | Residue | Details |
E | LYS7 | |
E | ARG10 | |
E | LYS41 | |
E | LYS66 | |
E | ARG85 |
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 |
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 |
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 |
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 |