4WYZ
The crystal structure of the A109G mutant of RNase A in complex with 3'UMP
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | binding site for residue U3P A 401 |
Chain | Residue |
A | GLN11 |
A | HOH508 |
A | HOH528 |
A | HOH536 |
A | HOH553 |
A | HOH555 |
A | HOH574 |
A | HOH590 |
A | HOH593 |
A | HOH612 |
A | HOH620 |
A | HIS12 |
A | HOH649 |
A | LYS41 |
A | VAL43 |
A | ASN44 |
A | THR45 |
A | PHE120 |
A | ASP121 |
A | HOH502 |
site_id | AC2 |
Number of Residues | 22 |
Details | binding site for residue U3P B 401 |
Chain | Residue |
B | GLN11 |
B | HIS12 |
B | SER15 |
B | SER16 |
B | THR17 |
B | SER18 |
B | LYS41 |
B | VAL43 |
B | ASN44 |
B | THR45 |
B | HIS119 |
B | PHE120 |
B | ASP121 |
B | ALA122 |
B | HOH520 |
B | HOH539 |
B | HOH551 |
B | HOH574 |
B | HOH616 |
B | HOH623 |
B | HOH646 |
B | HOH659 |
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 | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | HIS12 | |
B | HIS12 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | HIS119 | |
B | HIS119 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: |
Chain | Residue | Details |
B | LYS66 | |
B | ARG85 | |
A | LYS7 | |
A | ARG10 | |
A | LYS41 | |
A | LYS66 | |
A | ARG85 | |
B | LYS7 | |
B | ARG10 | |
B | LYS41 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | CARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761 |
Chain | Residue | Details |
A | LYS1 | |
A | LYS7 | |
A | LYS37 | |
A | LYS41 | |
B | LYS1 | |
B | LYS7 | |
B | LYS37 | |
B | LYS41 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:19358553 |
Chain | Residue | Details |
A | ASN34 | |
B | 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 |