7AG7
Crystal structure of SFP aldolase YihT from Salmonella enterica in complex with sulfate bound at the active site
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016829 | molecular_function | lyase activity |
A | 0061595 | molecular_function | 6-deoxy-6-sulfofructose-1-phosphate aldolase activity |
A | 1902777 | biological_process | 6-sulfoquinovose(1-) catabolic process |
B | 0016829 | molecular_function | lyase activity |
B | 0061595 | molecular_function | 6-deoxy-6-sulfofructose-1-phosphate aldolase activity |
B | 1902777 | biological_process | 6-sulfoquinovose(1-) catabolic process |
C | 0016829 | molecular_function | lyase activity |
C | 0061595 | molecular_function | 6-deoxy-6-sulfofructose-1-phosphate aldolase activity |
C | 1902777 | biological_process | 6-sulfoquinovose(1-) catabolic process |
D | 0016829 | molecular_function | lyase activity |
D | 0061595 | molecular_function | 6-deoxy-6-sulfofructose-1-phosphate aldolase activity |
D | 1902777 | biological_process | 6-sulfoquinovose(1-) catabolic process |
E | 0016829 | molecular_function | lyase activity |
E | 0061595 | molecular_function | 6-deoxy-6-sulfofructose-1-phosphate aldolase activity |
E | 1902777 | biological_process | 6-sulfoquinovose(1-) catabolic process |
F | 0016829 | molecular_function | lyase activity |
F | 0061595 | molecular_function | 6-deoxy-6-sulfofructose-1-phosphate aldolase activity |
F | 1902777 | biological_process | 6-sulfoquinovose(1-) catabolic process |
G | 0016829 | molecular_function | lyase activity |
G | 0061595 | molecular_function | 6-deoxy-6-sulfofructose-1-phosphate aldolase activity |
G | 1902777 | biological_process | 6-sulfoquinovose(1-) catabolic process |
H | 0016829 | molecular_function | lyase activity |
H | 0061595 | molecular_function | 6-deoxy-6-sulfofructose-1-phosphate aldolase activity |
H | 1902777 | biological_process | 6-sulfoquinovose(1-) catabolic process |
I | 0016829 | molecular_function | lyase activity |
I | 0061595 | molecular_function | 6-deoxy-6-sulfofructose-1-phosphate aldolase activity |
I | 1902777 | biological_process | 6-sulfoquinovose(1-) catabolic process |
J | 0016829 | molecular_function | lyase activity |
J | 0061595 | molecular_function | 6-deoxy-6-sulfofructose-1-phosphate aldolase activity |
J | 1902777 | biological_process | 6-sulfoquinovose(1-) catabolic process |
K | 0016829 | molecular_function | lyase activity |
K | 0061595 | molecular_function | 6-deoxy-6-sulfofructose-1-phosphate aldolase activity |
K | 1902777 | biological_process | 6-sulfoquinovose(1-) catabolic process |
L | 0016829 | molecular_function | lyase activity |
L | 0061595 | molecular_function | 6-deoxy-6-sulfofructose-1-phosphate aldolase activity |
L | 1902777 | biological_process | 6-sulfoquinovose(1-) catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue SO4 A 301 |
Chain | Residue |
A | GLN23 |
A | LEU225 |
A | SER226 |
A | SER227 |
A | ALA251 |
A | GLY252 |
A | ARG253 |
A | HOH450 |
A | HOH476 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue SO4 B 301 |
Chain | Residue |
B | GLN23 |
B | LEU225 |
B | SER226 |
B | SER227 |
B | ALA251 |
B | GLY252 |
B | ARG253 |
B | HOH415 |
B | HOH422 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue SO4 C 301 |
Chain | Residue |
C | GLN23 |
C | LEU225 |
C | SER226 |
C | SER227 |
C | ALA251 |
C | GLY252 |
C | ARG253 |
C | HOH446 |
C | HOH448 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue SO4 D 301 |
Chain | Residue |
D | GLN23 |
D | LEU225 |
D | SER226 |
D | SER227 |
D | ALA251 |
D | GLY252 |
D | ARG253 |
D | HOH443 |
D | HOH468 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue SO4 E 301 |
Chain | Residue |
E | GLN23 |
E | LEU225 |
E | SER226 |
E | SER227 |
E | ALA251 |
E | GLY252 |
E | ARG253 |
E | HOH427 |
E | HOH441 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue SO4 F 301 |
Chain | Residue |
F | GLN23 |
F | LEU225 |
F | SER226 |
F | SER227 |
F | ALA251 |
F | GLY252 |
F | ARG253 |
site_id | AC7 |
Number of Residues | 9 |
Details | binding site for residue SO4 G 301 |
Chain | Residue |
G | GLN23 |
G | LEU225 |
G | SER226 |
G | SER227 |
G | ALA251 |
G | GLY252 |
G | ARG253 |
G | HOH416 |
G | HOH427 |
site_id | AC8 |
Number of Residues | 9 |
Details | binding site for residue SO4 H 301 |
Chain | Residue |
H | GLN23 |
H | LEU225 |
H | SER226 |
H | SER227 |
H | ALA251 |
H | GLY252 |
H | ARG253 |
H | HOH413 |
H | HOH425 |
site_id | AC9 |
Number of Residues | 9 |
Details | binding site for residue SO4 I 301 |
Chain | Residue |
I | GLN23 |
I | LEU225 |
I | SER226 |
I | SER227 |
I | ALA251 |
I | GLY252 |
I | ARG253 |
I | HOH455 |
I | HOH468 |
site_id | AD1 |
Number of Residues | 9 |
Details | binding site for residue SO4 J 301 |
Chain | Residue |
J | GLN23 |
J | LEU225 |
J | SER226 |
J | SER227 |
J | ALA251 |
J | GLY252 |
J | ARG253 |
J | HOH429 |
J | HOH465 |
site_id | AD2 |
Number of Residues | 9 |
Details | binding site for residue SO4 K 301 |
Chain | Residue |
K | GLN23 |
K | LEU225 |
K | SER226 |
K | SER227 |
K | ALA251 |
K | GLY252 |
K | ARG253 |
K | HOH439 |
K | HOH467 |
site_id | AD3 |
Number of Residues | 9 |
Details | binding site for residue SO4 L 301 |
Chain | Residue |
L | SER226 |
L | SER227 |
L | ALA251 |
L | GLY252 |
L | ARG253 |
L | HOH440 |
L | HOH499 |
L | GLN23 |
L | LEU225 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | ACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_01912, ECO:0000269|PubMed:33791429, ECO:0007744|PDB:7NE2 |
Chain | Residue | Details |
A | LYS193 | |
J | LYS193 | |
K | LYS193 | |
L | LYS193 | |
B | LYS193 | |
C | LYS193 | |
D | LYS193 | |
E | LYS193 | |
F | LYS193 | |
G | LYS193 | |
H | LYS193 | |
I | LYS193 |