1Z6D
Ribonuclease A- IMP complex
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 | 0003676 | molecular_function | nucleic acid binding |
B | 0004518 | molecular_function | nuclease activity |
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 | 0016787 | molecular_function | hydrolase activity |
B | 0016829 | molecular_function | lyase activity |
B | 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 IMP A 919 |
Chain | Residue |
A | LYS7 |
A | HOH988 |
A | HOH1002 |
A | HOH1081 |
A | HOH1083 |
A | HOH1099 |
A | HOH1111 |
A | GLN11 |
A | HIS12 |
A | LYS41 |
A | GLU111 |
A | VAL118 |
A | HIS119 |
A | PHE120 |
A | IMP920 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE IMP A 920 |
Chain | Residue |
A | HIS12 |
A | VAL43 |
A | ASN44 |
A | THR45 |
A | LYS66 |
A | ARG85 |
A | PHE120 |
A | ASP121 |
A | ALA122 |
A | IMP919 |
A | IMP921 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE IMP A 921 |
Chain | Residue |
A | LYS66 |
A | SER123 |
A | VAL124 |
A | IMP920 |
A | HOH959 |
A | HOH960 |
A | HOH996 |
A | HOH1022 |
B | SER59 |
B | GLN60 |
B | TYR76 |
B | HOH2044 |
B | HOH2069 |
site_id | AC4 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE IMP B 1920 |
Chain | Residue |
B | HIS12 |
B | VAL43 |
B | ASN44 |
B | THR45 |
B | LYS66 |
B | ARG85 |
B | PHE120 |
B | ASP121 |
B | ASP121 |
B | ALA122 |
B | ALA122 |
B | SER123 |
B | SER123 |
B | IMP1921 |
B | HOH2035 |
B | HOH2036 |
B | HOH2037 |
B | HOH2066 |
B | HOH2090 |
site_id | AC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE IMP B 1921 |
Chain | Residue |
A | HOH1007 |
B | ALA4 |
B | LYS7 |
B | GLN11 |
B | HIS12 |
B | LYS41 |
B | HIS119 |
B | PHE120 |
B | IMP1920 |
B | HOH1969 |
B | HOH2010 |
B | HOH2012 |
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 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | Binding site: {} |
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 |
Chain | Residue | Details |
A | PHE120 | |
A | HIS119 | |
A | HIS12 | |
A | LYS41 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1rbn |
Chain | Residue | Details |
B | PHE120 | |
B | HIS119 | |
B | HIS12 | |
B | LYS41 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1rbn |
Chain | Residue | Details |
A | HIS119 | |
A | HIS12 | |
A | LYS41 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1rbn |
Chain | Residue | Details |
B | HIS119 | |
B | HIS12 | |
B | LYS41 |
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 |