2ZKU
Structure of hepatitis C virus NS5B polymerase in a new crystal form
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003723 | molecular_function | RNA binding |
A | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
A | 0039694 | biological_process | viral RNA genome replication |
B | 0003723 | molecular_function | RNA binding |
B | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
B | 0039694 | biological_process | viral RNA genome replication |
C | 0003723 | molecular_function | RNA binding |
C | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
C | 0039694 | biological_process | viral RNA genome replication |
D | 0003723 | molecular_function | RNA binding |
D | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
D | 0039694 | biological_process | viral RNA genome replication |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACY A 3001 |
Chain | Residue |
A | ARG501 |
A | TRP528 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACY A 3005 |
Chain | Residue |
A | ARG222 |
A | CYS223 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 4001 |
Chain | Residue |
A | ALA105 |
A | LYS106 |
A | PRO94 |
A | HIS95 |
A | SER96 |
A | LYS98 |
A | GLY104 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 4002 |
Chain | Residue |
A | ASP129 |
A | VAL131 |
A | THR132 |
D | LEU60 |
D | LEU68 |
D | ASN231 |
D | VAL235 |
D | HOH3008 |
D | HOH3303 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 4004 |
Chain | Residue |
A | PHE203 |
A | ASN206 |
A | THR207 |
A | SER210 |
A | THR312 |
A | HOH4007 |
A | HOH4190 |
B | ARG508 |
B | HOH4034 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 4005 |
Chain | Residue |
A | SER96 |
A | ALA97 |
A | ARG168 |
A | GLY557 |
A | HOH4108 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 4006 |
Chain | Residue |
A | GLU202 |
A | ASN206 |
A | LYS209 |
A | HOH4024 |
A | HOH4041 |
B | SER506 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACY B 3003 |
Chain | Residue |
B | ARG465 |
B | LEU547 |
site_id | AC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE ACY B 3004 |
Chain | Residue |
B | TRP408 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACY B 3007 |
Chain | Residue |
B | SER218 |
B | GLU357 |
B | LEU362 |
B | ILE363 |
B | THR364 |
B | HOH4524 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 4003 |
Chain | Residue |
B | PHE203 |
B | ASN206 |
B | THR207 |
B | HOH4036 |
B | HOH4114 |
D | ARG508 |
D | HOH3035 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 4007 |
Chain | Residue |
B | ALA97 |
B | ILE160 |
B | PHE162 |
B | ARG168 |
B | HOH4125 |
B | HOH4158 |
B | HOH4355 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACY C 3002 |
Chain | Residue |
A | HIS502 |
C | GLY198 |
C | GLN199 |
C | GLU202 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACY D 3006 |
Chain | Residue |
D | LEU474 |
D | ARG501 |
D | TRP528 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000305|PubMed:10557268, ECO:0000305|PubMed:11884572 |
Chain | Residue | Details |
A | ASP220 | |
D | ASP220 | |
D | ASP318 | |
D | ASP319 | |
A | ASP318 | |
A | ASP319 | |
B | ASP220 | |
B | ASP318 | |
B | ASP319 | |
C | ASP220 | |
C | ASP318 | |
C | ASP319 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine; by host => ECO:0000250|UniProtKB:P26662 |
Chain | Residue | Details |
A | SER29 | |
A | SER42 | |
B | SER29 | |
B | SER42 | |
C | SER29 | |
C | SER42 | |
D | SER29 | |
D | SER42 |