3MWR
Crystal structure of ribonuclease A tandem enzymes and their interaction with the cytosolic ribonuclease inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| 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 | 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 | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 255 |
| Chain | Residue |
| A | THR3 |
| A | ALA4 |
| A | ASN192 |
| A | HOH357 |
| A | HOH373 |
| A | HOH402 |
| A | HOH421 |
| A | HOH467 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 256 |
| Chain | Residue |
| A | HIS12 |
| A | VAL118 |
| A | HIS119 |
| A | PHE120 |
| A | HOH374 |
| A | HOH449 |
| A | HOH480 |
| A | GLN11 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 257 |
| Chain | Residue |
| A | GLN141 |
| A | HIS142 |
| A | LYS171 |
| A | VAL248 |
| A | HIS249 |
| A | PHE250 |
| A | HOH365 |
| A | HOH403 |
| A | HOH451 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 258 |
| Chain | Residue |
| A | ALA252 |
| A | ALA252 |
| A | SER253 |
| A | SER253 |
| A | HOH289 |
| A | HOH345 |
| A | HOH543 |
| A | HOH543 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 259 |
| Chain | Residue |
| A | SER153 |
| A | THR229 |
| A | THR230 |
| A | GLN231 |
| A | HOH576 |
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 | |
| A | CYS170-PHE176 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | HIS142 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | HIS249 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS137 | |
| A | ARG140 | |
| A | LYS171 | |
| A | LYS196 | |
| A | ARG215 |
| 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 | LYS131 | |
| A | LYS137 | |
| A | LYS167 | |
| A | LYS171 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:19358553 |
| Chain | Residue | Details |
| A | ASN164 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 164 |
| Chain | Residue | Details |
| A | HIS142 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | LYS171 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS249 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | PHE250 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP251 | electrostatic stabiliser, hydrogen bond acceptor |
