3AHS
Crystal Structure of Ustilago sphaerogena Ribonuclease U2B
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0033899 | molecular_function | ribonuclease U2 activity |
A | 0046872 | molecular_function | metal ion binding |
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 | 0033899 | molecular_function | ribonuclease U2 activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0003723 | molecular_function | RNA binding |
C | 0004518 | molecular_function | nuclease activity |
C | 0004519 | molecular_function | endonuclease activity |
C | 0004521 | molecular_function | RNA endonuclease activity |
C | 0004540 | molecular_function | RNA nuclease activity |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016829 | molecular_function | lyase activity |
C | 0033899 | molecular_function | ribonuclease U2 activity |
C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PO4 A 115 |
Chain | Residue |
A | TYR39 |
C | TYR78 |
A | HIS41 |
A | GLU62 |
A | ARG85 |
A | HIS101 |
A | PHE110 |
A | HOH247 |
A | HOH382 |
A | HOH488 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K A 116 |
Chain | Residue |
A | ASP28 |
A | VAL30 |
A | GLY33 |
A | HOH505 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PO4 B 115 |
Chain | Residue |
B | TYR39 |
B | HIS41 |
B | GLU62 |
B | TYR78 |
B | ARG85 |
B | HIS101 |
B | PHE110 |
B | HOH258 |
B | HOH282 |
B | HOH390 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K B 116 |
Chain | Residue |
B | ASP28 |
B | VAL30 |
B | GLY33 |
B | HOH427 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PO4 C 115 |
Chain | Residue |
A | TYR78 |
C | TYR39 |
C | HIS41 |
C | GLU62 |
C | ARG85 |
C | HIS101 |
C | PHE110 |
C | HOH305 |
C | HOH320 |
C | HOH438 |
site_id | AC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE GOL C 201 |
Chain | Residue |
B | GLY10 |
B | THR102 |
B | GLY103 |
B | THR111 |
C | GLY10 |
C | GLY11 |
C | ASN12 |
C | THR102 |
C | HOH294 |
C | HOH329 |
C | HOH367 |
C | HOH481 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 202 |
Chain | Residue |
A | TYR44 |
A | GLU46 |
A | HOH437 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | Active site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1973","firstPage":"453","lastPage":"472","publisher":"Publ. House Slovak Acad. Sci.","address":"Bratislava","bookName":"Ribosomes and RNA metabolism","editors":["Zelinka J.","Balan J."],"authors":["Uchida T.","Sato S."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1973","firstPage":"453","lastPage":"472","publisher":"Publ. House Slovak Acad. Sci.","address":"Bratislava","bookName":"Ribosomes and RNA metabolism","editors":["Zelinka J.","Balan J."],"authors":["Uchida T.","Sato S."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | Active site: {"description":"Proton donor","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1973","firstPage":"453","lastPage":"472","publisher":"Publ. House Slovak Acad. Sci.","address":"Bratislava","bookName":"Ribosomes and RNA metabolism","editors":["Zelinka J.","Balan J."],"authors":["Uchida T.","Sato S."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 14 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"20858208","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 39 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | Site: {"description":"Methylation inactivates enzyme","evidences":[{"source":"PubMed","id":"7492561","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 908 |
Chain | Residue | Details |
A | ASP45 | proton shuttle (general acid/base) |
A | VAL66 | proton shuttle (general acid/base) |
A | GLN89 | electrostatic stabiliser |
A | ALA105 | proton shuttle (general acid/base) |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 908 |
Chain | Residue | Details |
B | ASP45 | proton shuttle (general acid/base) |
B | VAL66 | proton shuttle (general acid/base) |
B | GLN89 | electrostatic stabiliser |
B | ALA105 | proton shuttle (general acid/base) |
site_id | MCSA3 |
Number of Residues | 4 |
Details | M-CSA 908 |
Chain | Residue | Details |
C | ASP45 | proton shuttle (general acid/base) |
C | VAL66 | proton shuttle (general acid/base) |
C | GLN89 | electrostatic stabiliser |
C | ALA105 | proton shuttle (general acid/base) |