Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001411 | cellular_component | hyphal tip |
A | 0003723 | molecular_function | RNA binding |
A | 0004518 | molecular_function | nuclease activity |
A | 0004519 | molecular_function | endonuclease activity |
A | 0004521 | molecular_function | RNA endonuclease activity |
A | 0004540 | molecular_function | RNA nuclease activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0030428 | cellular_component | cell septum |
A | 0046589 | molecular_function | ribonuclease T1 activity |
B | 0001411 | cellular_component | hyphal tip |
B | 0003723 | molecular_function | RNA binding |
B | 0004518 | molecular_function | nuclease activity |
B | 0004519 | molecular_function | endonuclease activity |
B | 0004521 | molecular_function | RNA endonuclease activity |
B | 0004540 | molecular_function | RNA nuclease activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016829 | molecular_function | lyase activity |
B | 0030428 | cellular_component | cell septum |
B | 0046589 | molecular_function | ribonuclease T1 activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA A 106 |
Chain | Residue |
A | ASP15 |
A | HOH468 |
A | HOH499 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 306 |
Chain | Residue |
B | ASP215 |
B | HOH414 |
B | HOH444 |
B | HOH456 |
B | HOH479 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 2GP A 105 |
Chain | Residue |
A | HIS40 |
A | LYS41 |
A | TYR42 |
A | ASN43 |
A | ASN44 |
A | TYR45 |
A | GLU46 |
A | GLU58 |
A | ARG77 |
A | HIS92 |
A | ASN98 |
A | PHE100 |
A | TYR38 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 2GP B 305 |
Chain | Residue |
B | TYR238 |
B | HIS240 |
B | TYR242 |
B | ASN243 |
B | ASN244 |
B | TYR245 |
B | GLU246 |
B | GLU258 |
B | ARG277 |
B | HIS292 |
B | ASN298 |
B | ASN299 |
B | PHE300 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"evidences":[{"source":"PubMed","id":"2844811","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"2844811","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton donor"} |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b2m |
Chain | Residue | Details |
A | GLU58 | |
A | HIS40 | |
A | HIS92 | |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b2m |
Chain | Residue | Details |
B | HIS292 | |
B | GLU258 | |
B | HIS240 | |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 414 |
Chain | Residue | Details |
A | TYR38 | electrostatic stabiliser |
A | HIS40 | proton shuttle (general acid/base) |
A | GLU58 | proton shuttle (general acid/base) |
A | ARG77 | electrostatic stabiliser |
A | HIS92 | proton shuttle (general acid/base) |
A | PHE100 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 414 |
Chain | Residue | Details |
B | TYR238 | electrostatic stabiliser |
B | HIS240 | proton shuttle (general acid/base) |
B | GLU258 | proton shuttle (general acid/base) |
B | ARG277 | electrostatic stabiliser |
B | HIS292 | proton shuttle (general acid/base) |
B | PHE300 | electrostatic stabiliser |