2P46
Complex of a camelid single-domain vhh antibody fragment with RNASE A at 2.5A resolution: se5b-ortho-2 crystal form with five se-met sites (L4M, M34, M51, F68M, M83) in vhh scaffold.
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 |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 201 |
| Chain | Residue |
| A | GLN11 |
| A | HIS12 |
| A | HIS119 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 202 |
| Chain | Residue |
| A | HIS105 |
| A | HOH206 |
| A | HOH207 |
| B | GLU102 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 203 |
| Chain | Residue |
| A | HOH209 |
| B | GLY56 |
| A | GLU49 |
| A | HOH208 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN A 204 |
| Chain | Residue |
| A | GLU49 |
| A | ASP53 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 205 |
| Chain | Residue |
| A | HIS119 |
| A | ASP121 |
| A | HOH210 |
| A | HOH211 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN C 207 |
| Chain | Residue |
| C | HIS12 |
| C | HIS119 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 208 |
| Chain | Residue |
| C | HIS105 |
| C | HOH211 |
| C | HOH212 |
| D | GLU102 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN C 209 |
| Chain | Residue |
| C | GLU49 |
| C | SER80 |
| D | HOH229 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 210 |
| Chain | Residue |
| C | HIS119 |
| C | ASP121 |
| C | HOH214 |
| C | HOH215 |
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 | |
| C | HIS12 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | HIS119 | |
| C | HIS119 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS7 | |
| C | ARG85 | |
| A | ARG10 | |
| A | LYS41 | |
| A | LYS66 | |
| A | ARG85 | |
| C | LYS7 | |
| C | ARG10 | |
| C | LYS41 | |
| C | LYS66 |
| 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 | |
| C | LYS1 | |
| C | LYS7 | |
| C | LYS37 | |
| C | 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 | |
| C | ASN34 |
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 |
| C | PHE120 | |
| C | HIS119 | |
| C | HIS12 | |
| C | 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 |
| C | HIS119 | |
| C | HIS12 | |
| C | 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 |
| 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 |
