1V9H
Crystal structure of the RNase MC1 mutant Y101A in complex with 5'-UMP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003723 | molecular_function | RNA binding |
A | 0004519 | molecular_function | endonuclease activity |
A | 0004521 | molecular_function | RNA endonuclease activity |
A | 0005576 | cellular_component | extracellular region |
A | 0006401 | biological_process | RNA catabolic process |
A | 0016829 | molecular_function | lyase activity |
A | 0033897 | molecular_function | ribonuclease T2 activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 A 301 |
Chain | Residue |
A | PRO52 |
A | PHE53 |
A | THR86 |
A | ARG132 |
A | GLY185 |
A | ALA186 |
A | HOH1030 |
A | HOH1043 |
A | HOH1068 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 302 |
Chain | Residue |
A | GLY35 |
A | LEU36 |
A | TRP69 |
A | GLU84 |
A | TRP85 |
A | GLY89 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 303 |
Chain | Residue |
A | ASN47 |
A | HIS83 |
A | LYS87 |
A | HOH1083 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE U5P A 1001 |
Chain | Residue |
A | GLN9 |
A | HIS34 |
A | ASN71 |
A | VAL72 |
A | LEU73 |
A | ARG74 |
A | PHE80 |
A | HIS83 |
A | GLU84 |
A | LYS87 |
A | HIS88 |
A | HOH1039 |
A | HOH1050 |
A | HOH1055 |
A | HOH1077 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10045, ECO:0000269|PubMed:12731868, ECO:0000269|PubMed:15322360, ECO:0000305|PubMed:10446375, ECO:0007744|PDB:1J1F, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1UCD, ECO:0007744|PDB:1V9H |
Chain | Residue | Details |
A | HIS34 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:10964705, ECO:0000269|PubMed:12731868, ECO:0000269|PubMed:15322360, ECO:0000305|PubMed:10446375, ECO:0007744|PDB:1J1F, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1UCA, ECO:0007744|PDB:1UCD, ECO:0007744|PDB:1V9H |
Chain | Residue | Details |
A | TRP85 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10045, ECO:0000269|PubMed:12731868, ECO:0000269|PubMed:15322360, ECO:0000305|PubMed:10446375, ECO:0007744|PDB:1J1F, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1UCD, ECO:0007744|PDB:1V9H |
Chain | Residue | Details |
A | GLY89 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:10964705, ECO:0000305|PubMed:12731868, ECO:0000305|PubMed:15322360, ECO:0007744|PDB:1J1F, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1UCA, ECO:0007744|PDB:1UCC, ECO:0007744|PDB:1UCD, ECO:0007744|PDB:1V9H |
Chain | Residue | Details |
A | GLN9 | |
A | VAL72 | |
A | HIS88 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12731868, ECO:0000269|PubMed:15322360, ECO:0007744|PDB:1J1F, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1UCD, ECO:0007744|PDB:1V9H |
Chain | Residue | Details |
A | HIS34 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15322360, ECO:0000305|PubMed:12731868, ECO:0007744|PDB:1J1F, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1V9H |
Chain | Residue | Details |
A | ALA75 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15322360, ECO:0000305|PubMed:10964705, ECO:0000305|PubMed:12731868, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1UCA, ECO:0007744|PDB:1UCD, ECO:0007744|PDB:1V9H |
Chain | Residue | Details |
A | TRP81 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:10964705, ECO:0000305|PubMed:12731868, ECO:0000305|PubMed:15322360, ECO:0007744|PDB:1J1F, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1UCA, ECO:0007744|PDB:1UCD, ECO:0007744|PDB:1V9H |
Chain | Residue | Details |
A | GLU84 |
site_id | SWS_FT_FI9 |
Number of Residues | 9 |
Details | SITE: Involved in thermostability => ECO:0000269|PubMed:15322360 |
Chain | Residue | Details |
A | PHE102 | |
A | LYS103 | |
A | VAL106 | |
A | ASN126 | |
A | ARG128 | |
A | LYS145 | |
A | VAL163 | |
A | VAL166 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bol |
Chain | Residue | Details |
A | HIS34 | |
A | GLU84 | |
A | HIS88 |