3FEQ
Crystal structure of uncharacterized protein eah89906
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
A | 0046872 | molecular_function | metal ion binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
B | 0046872 | molecular_function | metal ion binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
C | 0046872 | molecular_function | metal ion binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0016787 | molecular_function | hydrolase activity |
D | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
D | 0046872 | molecular_function | metal ion binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0016787 | molecular_function | hydrolase activity |
E | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
E | 0046872 | molecular_function | metal ion binding |
F | 0005737 | cellular_component | cytoplasm |
F | 0016787 | molecular_function | hydrolase activity |
F | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
F | 0046872 | molecular_function | metal ion binding |
G | 0005737 | cellular_component | cytoplasm |
G | 0016787 | molecular_function | hydrolase activity |
G | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
G | 0046872 | molecular_function | metal ion binding |
H | 0005737 | cellular_component | cytoplasm |
H | 0016787 | molecular_function | hydrolase activity |
H | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
H | 0046872 | molecular_function | metal ion binding |
I | 0005737 | cellular_component | cytoplasm |
I | 0016787 | molecular_function | hydrolase activity |
I | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
I | 0046872 | molecular_function | metal ion binding |
J | 0005737 | cellular_component | cytoplasm |
J | 0016787 | molecular_function | hydrolase activity |
J | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
J | 0046872 | molecular_function | metal ion binding |
K | 0005737 | cellular_component | cytoplasm |
K | 0016787 | molecular_function | hydrolase activity |
K | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
K | 0046872 | molecular_function | metal ion binding |
L | 0005737 | cellular_component | cytoplasm |
L | 0016787 | molecular_function | hydrolase activity |
L | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
L | 0046872 | molecular_function | metal ion binding |
M | 0005737 | cellular_component | cytoplasm |
M | 0016787 | molecular_function | hydrolase activity |
M | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
M | 0046872 | molecular_function | metal ion binding |
N | 0005737 | cellular_component | cytoplasm |
N | 0016787 | molecular_function | hydrolase activity |
N | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
N | 0046872 | molecular_function | metal ion binding |
O | 0005737 | cellular_component | cytoplasm |
O | 0016787 | molecular_function | hydrolase activity |
O | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
O | 0046872 | molecular_function | metal ion binding |
P | 0005737 | cellular_component | cytoplasm |
P | 0016787 | molecular_function | hydrolase activity |
P | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
P | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 425 |
Chain | Residue |
A | HIS63 |
A | HIS65 |
A | LYS188 |
A | ASP321 |
A | ZN426 |
A | HOH437 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 426 |
Chain | Residue |
A | HIS249 |
A | ZN425 |
A | HOH437 |
A | HIS63 |
A | LYS188 |
A | HIS229 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN B 425 |
Chain | Residue |
B | HIS63 |
B | HIS65 |
B | LYS188 |
B | ASP321 |
B | ZN426 |
B | HOH445 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 426 |
Chain | Residue |
B | LYS188 |
B | HIS229 |
B | HIS249 |
B | ZN425 |
B | HOH445 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN C 425 |
Chain | Residue |
C | HIS63 |
C | HIS65 |
C | LYS188 |
C | ASP321 |
C | HOH422 |
C | ZN426 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 426 |
Chain | Residue |
C | LYS188 |
C | HIS229 |
C | HIS249 |
C | HOH422 |
C | ZN425 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN D 425 |
Chain | Residue |
D | HIS63 |
D | HIS65 |
D | LYS188 |
D | ASP321 |
D | ZN426 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 426 |
Chain | Residue |
D | LYS188 |
D | HIS229 |
D | HIS249 |
D | ZN425 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN E 425 |
Chain | Residue |
E | HIS63 |
E | HIS65 |
E | LYS188 |
E | ASP321 |
E | ZN426 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN E 426 |
Chain | Residue |
E | LYS188 |
E | HIS229 |
E | HIS249 |
E | ZN425 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN F 425 |
Chain | Residue |
F | HIS63 |
F | HIS65 |
F | LYS188 |
F | ASP321 |
F | ZN426 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN F 426 |
Chain | Residue |
F | LYS188 |
F | HIS229 |
F | HIS249 |
F | ZN425 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN G 425 |
Chain | Residue |
G | HIS63 |
G | HIS65 |
G | LYS188 |
G | ASP321 |
G | ZN426 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN G 426 |
Chain | Residue |
G | LYS188 |
G | HIS229 |
G | HIS249 |
G | ZN425 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN H 425 |
Chain | Residue |
H | HIS63 |
H | HIS65 |
H | LYS188 |
H | ASP321 |
H | ZN426 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN H 426 |
Chain | Residue |
H | LYS188 |
H | HIS229 |
H | HIS249 |
H | ZN425 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN I 425 |
Chain | Residue |
I | HIS63 |
I | HIS65 |
I | LYS188 |
I | ASP321 |
I | ZN426 |
site_id | BC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN I 426 |
Chain | Residue |
I | HIS140 |
I | LYS188 |
I | HIS229 |
I | HIS249 |
I | ZN425 |
site_id | CC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN J 425 |
Chain | Residue |
J | HIS63 |
J | HIS65 |
J | LYS188 |
J | ASP321 |
J | ZN426 |
site_id | CC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN J 426 |
Chain | Residue |
J | LYS188 |
J | HIS229 |
J | HIS249 |
J | ZN425 |
site_id | CC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN K 425 |
Chain | Residue |
K | HIS65 |
K | LYS188 |
K | ASP321 |
K | ZN426 |
K | HIS63 |
site_id | CC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN K 426 |
Chain | Residue |
K | LYS188 |
K | HIS229 |
K | HIS249 |
K | ZN425 |
site_id | CC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN L 425 |
Chain | Residue |
L | HIS63 |
L | HIS65 |
L | LYS188 |
L | ASP321 |
L | ZN426 |
site_id | CC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN L 426 |
Chain | Residue |
L | HIS63 |
L | LYS188 |
L | HIS229 |
L | HIS249 |
L | ZN425 |
site_id | CC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN M 425 |
Chain | Residue |
M | HIS63 |
M | HIS65 |
M | LYS188 |
M | ASP321 |
M | ZN426 |
site_id | CC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN M 426 |
Chain | Residue |
M | LYS188 |
M | HIS229 |
M | HIS249 |
M | ZN425 |
site_id | CC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN N 425 |
Chain | Residue |
N | HIS63 |
N | HIS65 |
N | LYS188 |
N | ASP321 |
N | ZN426 |
site_id | DC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN N 426 |
Chain | Residue |
N | HIS140 |
N | HIS229 |
N | HIS249 |
N | ZN425 |
site_id | DC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN O 425 |
Chain | Residue |
O | HIS63 |
O | HIS65 |
O | LYS188 |
O | ASP321 |
O | ZN426 |
site_id | DC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN O 426 |
Chain | Residue |
O | LYS188 |
O | HIS229 |
O | HIS249 |
O | ZN425 |
site_id | DC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN P 425 |
Chain | Residue |
P | HIS63 |
P | HIS65 |
P | LYS188 |
P | ASP321 |
P | ZN426 |
site_id | DC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN P 426 |
Chain | Residue |
P | HIS63 |
P | LYS188 |
P | HIS229 |
P | HIS249 |
P | ZN425 |