4BLO
P4 PROTEIN FROM BACTERIOPHAGE PHI6 IN COMPLEX WITH ADP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0016787 | molecular_function | hydrolase activity |
A | 0017111 | molecular_function | ribonucleoside triphosphate phosphatase activity |
A | 0019028 | cellular_component | viral capsid |
A | 0019072 | biological_process | viral genome packaging |
A | 0046729 | cellular_component | viral procapsid |
B | 0005524 | molecular_function | ATP binding |
B | 0016787 | molecular_function | hydrolase activity |
B | 0017111 | molecular_function | ribonucleoside triphosphate phosphatase activity |
B | 0019028 | cellular_component | viral capsid |
B | 0019072 | biological_process | viral genome packaging |
B | 0046729 | cellular_component | viral procapsid |
C | 0005524 | molecular_function | ATP binding |
C | 0016787 | molecular_function | hydrolase activity |
C | 0017111 | molecular_function | ribonucleoside triphosphate phosphatase activity |
C | 0019028 | cellular_component | viral capsid |
C | 0019072 | biological_process | viral genome packaging |
C | 0046729 | cellular_component | viral procapsid |
D | 0005524 | molecular_function | ATP binding |
D | 0016787 | molecular_function | hydrolase activity |
D | 0017111 | molecular_function | ribonucleoside triphosphate phosphatase activity |
D | 0019028 | cellular_component | viral capsid |
D | 0019072 | biological_process | viral genome packaging |
D | 0046729 | cellular_component | viral procapsid |
E | 0005524 | molecular_function | ATP binding |
E | 0016787 | molecular_function | hydrolase activity |
E | 0017111 | molecular_function | ribonucleoside triphosphate phosphatase activity |
E | 0019028 | cellular_component | viral capsid |
E | 0019072 | biological_process | viral genome packaging |
E | 0046729 | cellular_component | viral procapsid |
F | 0005524 | molecular_function | ATP binding |
F | 0016787 | molecular_function | hydrolase activity |
F | 0017111 | molecular_function | ribonucleoside triphosphate phosphatase activity |
F | 0019028 | cellular_component | viral capsid |
F | 0019072 | biological_process | viral genome packaging |
F | 0046729 | cellular_component | viral procapsid |
G | 0005524 | molecular_function | ATP binding |
G | 0016787 | molecular_function | hydrolase activity |
G | 0017111 | molecular_function | ribonucleoside triphosphate phosphatase activity |
G | 0019028 | cellular_component | viral capsid |
G | 0019072 | biological_process | viral genome packaging |
G | 0046729 | cellular_component | viral procapsid |
H | 0005524 | molecular_function | ATP binding |
H | 0016787 | molecular_function | hydrolase activity |
H | 0017111 | molecular_function | ribonucleoside triphosphate phosphatase activity |
H | 0019028 | cellular_component | viral capsid |
H | 0019072 | biological_process | viral genome packaging |
H | 0046729 | cellular_component | viral procapsid |
I | 0005524 | molecular_function | ATP binding |
I | 0016787 | molecular_function | hydrolase activity |
I | 0017111 | molecular_function | ribonucleoside triphosphate phosphatase activity |
I | 0019028 | cellular_component | viral capsid |
I | 0019072 | biological_process | viral genome packaging |
I | 0046729 | cellular_component | viral procapsid |
J | 0005524 | molecular_function | ATP binding |
J | 0016787 | molecular_function | hydrolase activity |
J | 0017111 | molecular_function | ribonucleoside triphosphate phosphatase activity |
J | 0019028 | cellular_component | viral capsid |
J | 0019072 | biological_process | viral genome packaging |
J | 0046729 | cellular_component | viral procapsid |
K | 0005524 | molecular_function | ATP binding |
K | 0016787 | molecular_function | hydrolase activity |
K | 0017111 | molecular_function | ribonucleoside triphosphate phosphatase activity |
K | 0019028 | cellular_component | viral capsid |
K | 0019072 | biological_process | viral genome packaging |
K | 0046729 | cellular_component | viral procapsid |
L | 0005524 | molecular_function | ATP binding |
L | 0016787 | molecular_function | hydrolase activity |
L | 0017111 | molecular_function | ribonucleoside triphosphate phosphatase activity |
L | 0019028 | cellular_component | viral capsid |
L | 0019072 | biological_process | viral genome packaging |
L | 0046729 | cellular_component | viral procapsid |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA A 400 |
Chain | Residue |
A | SER133 |
A | GLU150 |
A | ADP401 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ADP A 401 |
Chain | Residue |
A | ILE134 |
A | GLY260 |
A | CA400 |
L | ARG264 |
L | ARG273 |
L | PHE275 |
A | ALA127 |
A | GLY129 |
A | SER130 |
A | GLY131 |
A | LYS132 |
A | SER133 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA B 400 |
Chain | Residue |
B | SER133 |
B | GLU150 |
B | ADP401 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ADP B 401 |
Chain | Residue |
A | ARG264 |
A | ARG273 |
A | PHE275 |
B | ALA127 |
B | GLY129 |
B | SER130 |
B | GLY131 |
B | LYS132 |
B | SER133 |
B | ILE134 |
B | GLY260 |
B | CA400 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA C 400 |
Chain | Residue |
C | SER133 |
C | GLU150 |
C | GLU153 |
C | ADP401 |
site_id | AC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ADP C 401 |
Chain | Residue |
C | ALA127 |
C | GLY129 |
C | SER130 |
C | GLY131 |
C | LYS132 |
C | SER133 |
C | ILE134 |
C | GLY260 |
C | CA400 |
H | ARG273 |
H | PHE275 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA D 400 |
Chain | Residue |
D | SER133 |
D | GLU150 |
D | GLU153 |
D | ADP401 |
site_id | AC8 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ADP D 401 |
Chain | Residue |
C | ARG273 |
D | ALA127 |
D | GLY129 |
D | SER130 |
D | GLY131 |
D | LYS132 |
D | SER133 |
D | ILE134 |
D | GLY260 |
D | CA400 |
J | LYS71 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA E 400 |
Chain | Residue |
E | SER133 |
E | GLU150 |
E | ADP401 |
site_id | BC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ADP E 401 |
Chain | Residue |
D | ARG273 |
E | ALA127 |
E | GLY129 |
E | SER130 |
E | GLY131 |
E | LYS132 |
E | SER133 |
E | ILE134 |
E | GLY260 |
E | CA400 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA F 400 |
Chain | Residue |
F | SER133 |
F | GLU150 |
F | ADP401 |
site_id | BC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ADP F 401 |
Chain | Residue |
E | ARG273 |
E | PHE275 |
F | ALA127 |
F | GLY129 |
F | SER130 |
F | GLY131 |
F | LYS132 |
F | SER133 |
F | ILE134 |
F | GLY260 |
F | CA400 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA G 400 |
Chain | Residue |
G | SER133 |
G | GLU150 |
G | ADP401 |
site_id | BC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ADP G 401 |
Chain | Residue |
G | ILE134 |
G | GLY260 |
G | CA400 |
F | ARG264 |
F | ARG273 |
F | PHE275 |
G | ALA127 |
G | GLY129 |
G | SER130 |
G | GLY131 |
G | LYS132 |
G | SER133 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA H 400 |
Chain | Residue |
H | SER133 |
H | GLU150 |
H | GLU153 |
H | ADP401 |
site_id | BC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ADP H 401 |
Chain | Residue |
G | ARG273 |
H | ALA127 |
H | GLY129 |
H | SER130 |
H | GLY131 |
H | LYS132 |
H | SER133 |
H | ILE134 |
H | GLY260 |
H | CA400 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA I 400 |
Chain | Residue |
I | SER133 |
I | GLU150 |
I | GLU153 |
I | ADP401 |
site_id | BC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ADP I 401 |
Chain | Residue |
B | ARG273 |
B | PHE275 |
E | LYS71 |
I | GLY129 |
I | SER130 |
I | GLY131 |
I | LYS132 |
I | SER133 |
I | ILE134 |
I | CA400 |
site_id | CC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA J 400 |
Chain | Residue |
J | SER133 |
J | GLU150 |
J | ADP401 |
site_id | CC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ADP J 401 |
Chain | Residue |
I | ARG273 |
I | PHE275 |
J | ALA127 |
J | GLY129 |
J | SER130 |
J | GLY131 |
J | LYS132 |
J | SER133 |
J | ILE134 |
J | GLY260 |
J | CA400 |
site_id | CC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA K 400 |
Chain | Residue |
K | SER133 |
K | GLU150 |
K | GLU153 |
K | ADP401 |
site_id | CC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ADP K 401 |
Chain | Residue |
J | PHE275 |
K | ALA127 |
K | GLY129 |
K | SER130 |
K | GLY131 |
K | LYS132 |
K | SER133 |
K | ILE134 |
K | CA400 |
site_id | CC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA L 400 |
Chain | Residue |
L | SER133 |
L | GLU150 |
L | GLU153 |
L | ADP401 |
site_id | CC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ADP L 401 |
Chain | Residue |
K | ARG264 |
K | ARG273 |
L | GLY129 |
L | SER130 |
L | GLY131 |
L | LYS132 |
L | SER133 |
L | ILE134 |
L | GLY260 |
L | CA400 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLY126 | |
J | GLY126 | |
K | GLY126 | |
L | GLY126 | |
B | GLY126 | |
C | GLY126 | |
D | GLY126 | |
E | GLY126 | |
F | GLY126 | |
G | GLY126 | |
H | GLY126 | |
I | GLY126 |