5ET4
Structure of RNase A-K7H/R10H in complex with 3'-CMP
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 |
| B | 0003676 | molecular_function | nucleic acid binding |
| 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 | 0016829 | molecular_function | lyase activity |
| B | 0050830 | biological_process | defense response to Gram-positive bacterium |
| C | 0003676 | molecular_function | nucleic acid binding |
| C | 0004519 | molecular_function | endonuclease activity |
| C | 0004522 | molecular_function | ribonuclease A activity |
| C | 0004540 | molecular_function | RNA nuclease activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0016829 | molecular_function | lyase activity |
| C | 0050830 | biological_process | defense response to Gram-positive bacterium |
| D | 0003676 | molecular_function | nucleic acid binding |
| D | 0004519 | molecular_function | endonuclease activity |
| D | 0004522 | molecular_function | ribonuclease A activity |
| D | 0004540 | molecular_function | RNA nuclease activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005576 | cellular_component | extracellular region |
| D | 0016829 | molecular_function | lyase activity |
| D | 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 C3P A 500 |
| Chain | Residue |
| A | GLN11 |
| A | HOH604 |
| A | HOH607 |
| A | HOH629 |
| A | HOH630 |
| A | HOH642 |
| B | HOH636 |
| A | HIS12 |
| A | LYS41 |
| A | VAL43 |
| A | ASN44 |
| A | THR45 |
| A | LYS66 |
| A | HIS119 |
| A | PHE120 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue C3P B 500 |
| Chain | Residue |
| B | GLN11 |
| B | HIS12 |
| B | LYS41 |
| B | VAL43 |
| B | ASN44 |
| B | THR45 |
| B | HIS119 |
| B | PHE120 |
| B | HOH601 |
| B | HOH606 |
| B | HOH667 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue C3P C 201 |
| Chain | Residue |
| C | GLN11 |
| C | HIS12 |
| C | LYS41 |
| C | VAL43 |
| C | ASN44 |
| C | THR45 |
| C | HIS119 |
| C | PHE120 |
| C | ASP121 |
| C | HOH343 |
| C | HOH360 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MPD C 202 |
| Chain | Residue |
| C | THR99 |
| C | THR100 |
| C | GLN101 |
| D | SER15 |
| D | SER50 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue C3P D 400 |
| Chain | Residue |
| D | HIS7 |
| D | GLN11 |
| D | HIS12 |
| D | LYS41 |
| D | VAL43 |
| D | ASN44 |
| D | THR45 |
| D | HIS119 |
| D | PHE120 |
| D | HOH553 |
| D | HOH556 |
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 | 4 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | HIS12 | |
| B | HIS12 | |
| C | HIS12 | |
| D | HIS12 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | HIS119 | |
| B | HIS119 | |
| C | HIS119 | |
| D | HIS119 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | HIS7 | |
| B | ARG85 | |
| C | HIS7 | |
| C | HIS10 | |
| C | LYS41 | |
| C | LYS66 | |
| C | ARG85 | |
| D | HIS7 | |
| D | HIS10 | |
| D | LYS41 | |
| D | LYS66 | |
| A | HIS10 | |
| D | ARG85 | |
| A | LYS41 | |
| A | LYS66 | |
| A | ARG85 | |
| B | HIS7 | |
| B | HIS10 | |
| B | LYS41 | |
| B | LYS66 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | CARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761 |
| Chain | Residue | Details |
| A | LYS1 | |
| C | HIS7 | |
| C | LYS37 | |
| C | LYS41 | |
| D | LYS1 | |
| D | HIS7 | |
| D | LYS37 | |
| D | LYS41 | |
| A | HIS7 | |
| A | LYS37 | |
| A | LYS41 | |
| B | LYS1 | |
| B | HIS7 | |
| B | LYS37 | |
| B | LYS41 | |
| C | LYS1 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:19358553 |
| Chain | Residue | Details |
| A | ASN34 | |
| B | ASN34 | |
| C | ASN34 | |
| D | 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 |
| 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 |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 164 |
| Chain | Residue | Details |
| C | HIS12 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | LYS41 | electrostatic stabiliser, hydrogen bond donor |
| C | HIS119 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | PHE120 | electrostatic stabiliser, hydrogen bond donor |
| C | ASP121 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 164 |
| Chain | Residue | Details |
| D | HIS12 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | LYS41 | electrostatic stabiliser, hydrogen bond donor |
| D | HIS119 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | PHE120 | electrostatic stabiliser, hydrogen bond donor |
| D | ASP121 | electrostatic stabiliser, hydrogen bond acceptor |
