3ZED
X-ray structure of the birnavirus VP1-VP3 complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0001172 | biological_process | RNA-templated transcription |
A | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
A | 0005525 | molecular_function | GTP binding |
A | 0016740 | molecular_function | transferase activity |
A | 0016779 | molecular_function | nucleotidyltransferase activity |
A | 0019079 | biological_process | viral genome replication |
A | 0034062 | molecular_function | 5'-3' RNA polymerase activity |
A | 0044423 | cellular_component | virion component |
B | 0000166 | molecular_function | nucleotide binding |
B | 0001172 | biological_process | RNA-templated transcription |
B | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
B | 0005525 | molecular_function | GTP binding |
B | 0016740 | molecular_function | transferase activity |
B | 0016779 | molecular_function | nucleotidyltransferase activity |
B | 0019079 | biological_process | viral genome replication |
B | 0034062 | molecular_function | 5'-3' RNA polymerase activity |
B | 0044423 | cellular_component | virion component |
C | 0000166 | molecular_function | nucleotide binding |
C | 0001172 | biological_process | RNA-templated transcription |
C | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
C | 0005525 | molecular_function | GTP binding |
C | 0016740 | molecular_function | transferase activity |
C | 0016779 | molecular_function | nucleotidyltransferase activity |
C | 0019079 | biological_process | viral genome replication |
C | 0034062 | molecular_function | 5'-3' RNA polymerase activity |
C | 0044423 | cellular_component | virion component |
D | 0005198 | molecular_function | structural molecule activity |
E | 0005198 | molecular_function | structural molecule activity |
F | 0005198 | molecular_function | structural molecule activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 1001 |
Chain | Residue |
A | LYS256 |
A | TRP322 |
A | ALA324 |
A | HIS329 |
A | GLY472 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K A 1002 |
Chain | Residue |
A | GLY512 |
A | ASN514 |
A | VAL177 |
A | ASN182 |
A | ASN184 |
A | ASN409 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K A 1003 |
Chain | Residue |
A | GLN203 |
A | THR698 |
A | SER701 |
A | PRO702 |
A | LYS704 |
A | HOH2274 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 1004 |
Chain | Residue |
A | GLN351 |
A | THR352 |
A | VAL383 |
A | ARG695 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K B 1002 |
Chain | Residue |
B | VAL177 |
B | ASN182 |
B | ASN184 |
B | ASN409 |
B | GLY512 |
B | ASN514 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K B 1003 |
Chain | Residue |
B | GLN203 |
B | THR698 |
B | SER701 |
B | PRO702 |
B | LYS704 |
B | HOH2162 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 1001 |
Chain | Residue |
C | LYS256 |
C | TRP322 |
C | ALA324 |
C | HIS329 |
C | GLY472 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K C 1002 |
Chain | Residue |
C | VAL177 |
C | ASN182 |
C | ASN184 |
C | ASN409 |
C | GLY512 |
C | ASN514 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K C 1003 |
Chain | Residue |
C | GLN203 |
C | THR698 |
C | SER701 |
C | PRO702 |
C | LYS704 |
C | HOH2163 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
A | GLY248 | |
B | GLY248 | |
C | GLY248 |