3KLF
Crystal structure of wild-type HIV-1 Reverse Transcriptase crosslinked to a DSDNA with a bound excision product, AZTPPPPA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
A | 0004523 | molecular_function | RNA-DNA hybrid ribonuclease activity |
A | 0006278 | biological_process | RNA-templated DNA biosynthetic process |
B | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
B | 0006278 | biological_process | RNA-templated DNA biosynthetic process |
E | 0003676 | molecular_function | nucleic acid binding |
E | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
E | 0004523 | molecular_function | RNA-DNA hybrid ribonuclease activity |
E | 0006278 | biological_process | RNA-templated DNA biosynthetic process |
F | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
F | 0006278 | biological_process | RNA-templated DNA biosynthetic process |
I | 0003676 | molecular_function | nucleic acid binding |
I | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
I | 0004523 | molecular_function | RNA-DNA hybrid ribonuclease activity |
I | 0006278 | biological_process | RNA-templated DNA biosynthetic process |
J | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
J | 0006278 | biological_process | RNA-templated DNA biosynthetic process |
M | 0003676 | molecular_function | nucleic acid binding |
M | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
M | 0004523 | molecular_function | RNA-DNA hybrid ribonuclease activity |
M | 0006278 | biological_process | RNA-templated DNA biosynthetic process |
N | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
N | 0006278 | biological_process | RNA-templated DNA biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 600 |
Chain | Residue |
A | ASP110 |
A | VAL111 |
A | ASP185 |
A | ZP4823 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 602 |
Chain | Residue |
A | ASP443 |
A | GLY444 |
A | ASP498 |
A | ASP549 |
A | HOH567 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE ZP4 A 823 |
Chain | Residue |
A | LYS65 |
A | ARG72 |
A | ASP110 |
A | VAL111 |
A | GLY112 |
A | ASP113 |
A | ALA114 |
A | TYR115 |
A | PHE116 |
A | GLN151 |
A | MET184 |
A | ASP185 |
A | LYS219 |
A | HOH560 |
A | MG600 |
C | DA705 |
D | 2DA822 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 429 |
Chain | Residue |
B | ARG78 |
B | GLU79 |
B | LYS82 |
B | GLU413 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG E 600 |
Chain | Residue |
E | ASP110 |
E | VAL111 |
E | ASP185 |
E | ZP4823 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG E 602 |
Chain | Residue |
E | ASP443 |
E | GLY444 |
E | ASP498 |
site_id | AC7 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE ZP4 E 823 |
Chain | Residue |
E | LYS65 |
E | LYS66 |
E | ARG72 |
E | ASP110 |
E | VAL111 |
E | GLY112 |
E | ASP113 |
E | ALA114 |
E | TYR115 |
E | PHE116 |
E | GLN151 |
E | MET184 |
E | ASP185 |
E | HIS221 |
E | LEU228 |
E | MG600 |
G | DA705 |
H | 2DA822 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL F 429 |
Chain | Residue |
F | ARG78 |
F | GLU79 |
F | GLU413 |
F | HOH433 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG I 600 |
Chain | Residue |
I | ASP110 |
I | VAL111 |
I | ASP185 |
I | ZP4823 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG I 602 |
Chain | Residue |
I | ASP443 |
I | GLY444 |
I | GLU478 |
I | ASP498 |
I | HOH565 |
site_id | BC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE ZP4 I 823 |
Chain | Residue |
I | LYS65 |
I | ARG72 |
I | ASP110 |
I | VAL111 |
I | ASP113 |
I | ALA114 |
I | TYR115 |
I | PHE116 |
I | GLN151 |
I | MET184 |
I | ASP185 |
I | HIS221 |
I | LEU228 |
I | HOH564 |
I | MG600 |
K | DA705 |
L | 2DA822 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG M 600 |
Chain | Residue |
M | ASP110 |
M | VAL111 |
M | GLY112 |
M | ASP185 |
M | ZP4823 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG M 602 |
Chain | Residue |
M | ASP443 |
M | GLU478 |
M | ASP498 |
M | HOH558 |
site_id | BC5 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ZP4 M 823 |
Chain | Residue |
M | ALA114 |
M | TYR115 |
M | PHE116 |
M | GLN151 |
M | MET184 |
M | ASP185 |
M | LYS219 |
M | MG600 |
O | DA705 |
P | 2DA822 |
M | LYS65 |
M | ARG72 |
M | ASP110 |
M | VAL111 |
M | ASP113 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: |
Chain | Residue | Details |
B | ASP110 | |
N | ASP110 | |
N | ASP185 | |
N | ASP186 | |
B | ASP185 | |
B | ASP186 | |
F | ASP110 | |
F | ASP185 | |
F | ASP186 | |
J | ASP110 | |
J | ASP185 | |
J | ASP186 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | SITE: Essential for RT p66/p51 heterodimerization |
Chain | Residue | Details |
B | TRP401 | |
I | GLU478 | |
I | ASP498 | |
I | ASP549 | |
M | ASP443 | |
M | GLU478 | |
M | ASP498 | |
M | ASP549 | |
B | TRP414 | |
F | TRP401 | |
F | TRP414 | |
J | TRP401 | |
J | TRP414 | |
N | TRP401 | |
N | TRP414 | |
I | ASP443 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | SITE: Essential for RT p66/p51 heterodimerization |
Chain | Residue | Details |
A | TRP401 | |
A | TRP414 | |
E | TRP401 | |
E | TRP414 | |
I | TRP401 | |
I | TRP414 | |
M | TRP401 | |
M | TRP414 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Cleavage; by viral protease; partial |
Chain | Residue | Details |
A | PHE440 | |
E | PHE440 | |
I | PHE440 | |
M | PHE440 |