5VE2
Crystal structure of enoyl-CoA hydratase/isomerase from Pseudoalteromonas atlantica T6c at 2.3 A resolution.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004300 | molecular_function | enoyl-CoA hydratase activity |
A | 0016829 | molecular_function | lyase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0004300 | molecular_function | enoyl-CoA hydratase activity |
B | 0016829 | molecular_function | lyase activity |
C | 0003824 | molecular_function | catalytic activity |
C | 0004300 | molecular_function | enoyl-CoA hydratase activity |
C | 0016829 | molecular_function | lyase activity |
D | 0003824 | molecular_function | catalytic activity |
D | 0004300 | molecular_function | enoyl-CoA hydratase activity |
D | 0016829 | molecular_function | lyase activity |
E | 0003824 | molecular_function | catalytic activity |
E | 0004300 | molecular_function | enoyl-CoA hydratase activity |
E | 0016829 | molecular_function | lyase activity |
F | 0003824 | molecular_function | catalytic activity |
F | 0004300 | molecular_function | enoyl-CoA hydratase activity |
F | 0016829 | molecular_function | lyase activity |
G | 0003824 | molecular_function | catalytic activity |
G | 0004300 | molecular_function | enoyl-CoA hydratase activity |
G | 0016829 | molecular_function | lyase activity |
H | 0003824 | molecular_function | catalytic activity |
H | 0004300 | molecular_function | enoyl-CoA hydratase activity |
H | 0016829 | molecular_function | lyase activity |
I | 0003824 | molecular_function | catalytic activity |
I | 0004300 | molecular_function | enoyl-CoA hydratase activity |
I | 0016829 | molecular_function | lyase activity |
J | 0003824 | molecular_function | catalytic activity |
J | 0004300 | molecular_function | enoyl-CoA hydratase activity |
J | 0016829 | molecular_function | lyase activity |
K | 0003824 | molecular_function | catalytic activity |
K | 0004300 | molecular_function | enoyl-CoA hydratase activity |
K | 0016829 | molecular_function | lyase activity |
L | 0003824 | molecular_function | catalytic activity |
L | 0004300 | molecular_function | enoyl-CoA hydratase activity |
L | 0016829 | molecular_function | lyase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue NA A 301 |
Chain | Residue |
A | SER42 |
A | ASP45 |
A | ILE48 |
A | HOH403 |
A | HOH445 |
A | HOH506 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue NA B 301 |
Chain | Residue |
B | HOH427 |
B | HOH449 |
B | HOH506 |
B | SER42 |
B | ASP45 |
B | ILE48 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue NA C 301 |
Chain | Residue |
C | SER42 |
C | ASP45 |
C | ILE48 |
C | HOH435 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue 1PE C 302 |
Chain | Residue |
C | ASN64 |
C | ARG126 |
C | VAL132 |
C | HOH458 |
C | HOH483 |
C | HOH502 |
C | HOH540 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue NA D 301 |
Chain | Residue |
D | SER42 |
D | ASP45 |
D | ILE48 |
D | HOH461 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue 1PE D 302 |
Chain | Residue |
D | ARG126 |
D | HOH437 |
D | HOH460 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue GOL E 301 |
Chain | Residue |
E | LEU66 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue GOL E 302 |
Chain | Residue |
E | ARG126 |
E | HOH469 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue NA E 303 |
Chain | Residue |
E | SER42 |
E | ASP45 |
E | ILE48 |
E | HOH402 |
E | HOH407 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue NA F 301 |
Chain | Residue |
F | SER42 |
F | ASP45 |
F | ILE48 |
F | HOH412 |
F | HOH417 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue NA G 301 |
Chain | Residue |
G | SER42 |
G | ASP45 |
G | ILE48 |
G | HOH412 |
G | HOH426 |
site_id | AD3 |
Number of Residues | 2 |
Details | binding site for residue PEG G 302 |
Chain | Residue |
G | ARG126 |
G | HOH465 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue NA H 301 |
Chain | Residue |
H | SER42 |
H | ASP45 |
H | ILE48 |
H | HOH406 |
H | HOH414 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue PEG H 302 |
Chain | Residue |
H | ARG126 |
H | HOH450 |
H | HOH464 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue NA I 301 |
Chain | Residue |
I | SER42 |
I | ASP45 |
I | ILE48 |
I | HOH436 |
I | HOH445 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue NA J 301 |
Chain | Residue |
J | SER42 |
J | ASP45 |
J | ILE48 |
J | HOH418 |
J | HOH458 |
site_id | AD8 |
Number of Residues | 5 |
Details | binding site for residue NA K 301 |
Chain | Residue |
K | SER42 |
K | ASP45 |
K | ILE48 |
K | HOH428 |
K | HOH451 |
site_id | AD9 |
Number of Residues | 5 |
Details | binding site for residue NA L 301 |
Chain | Residue |
L | SER42 |
L | ASP45 |
L | ILE48 |
L | HOH431 |
L | HOH456 |