1QHC
CRYSTAL STRUCTURE OF RIBONUCLEASE A IN COMPLEX WITH 5'-PHOSPHO-2'-DEOXYURIDINE-3'-PYROPHOSPHATE ADENOSINE-3'-PHOSPHATE
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 | 21 |
| Details | BINDING SITE FOR RESIDUE PUA A 901 |
| Chain | Residue |
| A | LYS7 |
| A | GLN11 |
| A | HIS12 |
| A | LYS41 |
| A | VAL43 |
| A | ASN44 |
| A | THR45 |
| A | CYS65 |
| A | ASN67 |
| A | GLN69 |
| A | ASN71 |
| A | GLU111 |
| A | VAL118 |
| A | HIS119 |
| A | PHE120 |
| A | HOH915 |
| A | HOH949 |
| A | HOH961 |
| B | THR70 |
| B | GLY88 |
| B | LYS91 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE PUA B 902 |
| Chain | Residue |
| B | ALA4 |
| B | LYS7 |
| B | GLN11 |
| B | HIS12 |
| B | ASN44 |
| B | THR45 |
| B | CYS65 |
| B | LYS66 |
| B | ASN67 |
| B | GLN69 |
| B | ASN71 |
| B | ALA109 |
| B | VAL118 |
| B | HIS119 |
| B | PHE120 |
| B | ASP121 |
| B | HOH931 |
| B | HOH932 |
| B | HOH933 |
| B | HOH940 |
| B | HOH956 |
| B | HOH966 |
| site_id | CA1 |
| Number of Residues | 7 |
| Details | PDUPPA3'-P BINDS TO THE CAT SITE. |
| Chain | Residue |
| B | HIS12 |
| B | THR45 |
| B | ASN67 |
| B | HIS119 |
| B | PHE120 |
| B | LYS7 |
| B | GLN11 |
| site_id | CAT |
| Number of Residues | 7 |
| Details | PDUPPA3'-P BINDS TO THE CAT SITE. |
| Chain | Residue |
| A | LYS7 |
| A | GLN11 |
| A | HIS12 |
| A | THR45 |
| A | ASN67 |
| A | HIS119 |
| A | PHE120 |
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 |
