6RSA
NUCLEAR MAGNETIC RESONANCE AND NEUTRON DIFFRACTION STUDIES OF THE COMPLEX OF RIBONUCLEASE*A WITH URIDINE VANADATE, A TRANSITION-STATE ANALOGUE
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 10 |
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 | DOD322 |
A | DOD323 |
site_id | ACT |
Number of Residues | 9 |
Details | ACTIVE SITE OF THE ENZYME |
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 | 21 |
Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton donor"} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 25 |
Details | Signal: {"evidences":[{"source":"PubMed","id":"13989651","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14235531","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor"} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 8 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
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_FI11 |
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 |
A | PHE120 | |
A | HIS119 | |
A | HIS12 | |
A | LYS41 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1rbn |
Chain | Residue | Details |
A | HIS119 | |
A | HIS12 | |
A | LYS41 |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 164 |
Chain | Residue | Details |
A | ASP38 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | ASN67 | 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 |