5R4Q
PanDDA analysis group deposition -- Crystal Structure of HUMAN CLEAVAGE FACTOR IM in complex with NM466-1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003729 | molecular_function | mRNA binding |
| A | 0005849 | cellular_component | mRNA cleavage factor complex |
| A | 0031124 | biological_process | mRNA 3'-end processing |
| B | 0003729 | molecular_function | mRNA binding |
| B | 0005849 | cellular_component | mRNA cleavage factor complex |
| B | 0031124 | biological_process | mRNA 3'-end processing |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | MET76 |
| A | TRP149 |
| A | HIS171 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue ZN A 302 |
| Chain | Residue |
| A | HIS89 |
| B | GLU200 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue ACT A 303 |
| Chain | Residue |
| A | PHE222 |
| A | HOH405 |
| A | HOH409 |
| A | GLU34 |
| A | ASN147 |
| A | HIS171 |
| A | LYS173 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 304 |
| Chain | Residue |
| A | PHE199 |
| A | TYR202 |
| A | ASP203 |
| A | ASN204 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| A | HIS89 |
| A | HOH406 |
| B | GLU88 |
| B | HIS93 |
| B | HOH401 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue ZN B 302 |
| Chain | Residue |
| A | GLU88 |
| A | HIS93 |
| A | HOH401 |
| A | HOH402 |
| A | HOH521 |
| B | HIS164 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 303 |
| Chain | Residue |
| A | ALA195 |
| A | ALA196 |
| A | GLU200 |
| A | HOH484 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue ZN B 304 |
| Chain | Residue |
| B | TRP149 |
| B | HIS171 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue RW7 B 305 |
| Chain | Residue |
| B | LEU53 |
| B | GLY108 |
| B | GLY109 |
| B | ILE128 |
| B | TYR191 |
| B | HOH434 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 250 |
| Details | Domain: {"description":"Nudix hydrolase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00794","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 158 |
| Details | Region: {"description":"Necessary for interactions with PAPOLA and PABPN1","evidences":[{"source":"PubMed","id":"15169763","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Region: {"description":"Interaction with RNA","evidences":[{"source":"PubMed","id":"20479262","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21295486","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3MDG","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"3MDI","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"3Q2T","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 42 |
| Details | Motif: {"description":"Nudix box"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Site: {"description":"Interaction with RNA","evidences":[{"source":"PubMed","id":"20479262","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3MDG","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"3MDI","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
