1RUV
RIBONUCLEASE A-URIDINE VANADATE COMPLEX: HIGH RESOLUTION RESOLUTION X-RAY STRUCTURE (1.3 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE UVC A 125 |
| Chain | Residue |
| A | GLN11 |
| A | HIS12 |
| A | LYS41 |
| A | VAL43 |
| A | ASN44 |
| A | THR45 |
| A | HIS119 |
| A | PHE120 |
| A | HOH229 |
| A | HOH310 |
| A | HOH358 |
| A | HOH373 |
| A | HOH401 |
| A | HOH411 |
| A | HOH425 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE TBU A 126 |
| Chain | Residue |
| A | ALA20 |
| A | SER22 |
| A | THR99 |
| site_id | ACT |
| Number of Residues | 9 |
| Details | THE SITE IS DEFINED AS RESIDUES WITHIN 4 ANGSTROMS OF THE URIDINE VANADATE OR WHICH APPEAR TO INTERACT THROUGH HYDROGEN BONDING TO OTHER ACTIVE SITE COMPONENTS (ASP 121 AND SER 123). |
| Chain | Residue |
| A | HIS12 |
| A | LYS41 |
| A | VAL43 |
| A | ASN44 |
| A | THR45 |
| A | HIS119 |
| A | PHE120 |
| A | ASP121 |
| A | SER123 |
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 | 1 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | HIS12 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | HIS119 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS7 | |
| A | ARG10 | |
| A | LYS41 | |
| A | LYS66 | |
| A | 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 |
| A | LYS1 | |
| A | LYS7 | |
| A | LYS37 | |
| A | LYS41 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:19358553 |
| Chain | Residue | Details |
| A | 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 |
