5EY8
Structure of FadD32 from Mycobacterium smegmatis complexed to AMPC20
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0008610 | biological_process | lipid biosynthetic process |
A | 0008922 | molecular_function | long-chain fatty acid [acyl-carrier-protein] ligase activity |
A | 0016874 | molecular_function | ligase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0008610 | biological_process | lipid biosynthetic process |
B | 0008922 | molecular_function | long-chain fatty acid [acyl-carrier-protein] ligase activity |
B | 0016874 | molecular_function | ligase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006631 | biological_process | fatty acid metabolic process |
C | 0008610 | biological_process | lipid biosynthetic process |
C | 0008922 | molecular_function | long-chain fatty acid [acyl-carrier-protein] ligase activity |
C | 0016874 | molecular_function | ligase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006631 | biological_process | fatty acid metabolic process |
D | 0008610 | biological_process | lipid biosynthetic process |
D | 0008922 | molecular_function | long-chain fatty acid [acyl-carrier-protein] ligase activity |
D | 0016874 | molecular_function | ligase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0006631 | biological_process | fatty acid metabolic process |
E | 0008610 | biological_process | lipid biosynthetic process |
E | 0008922 | molecular_function | long-chain fatty acid [acyl-carrier-protein] ligase activity |
E | 0016874 | molecular_function | ligase activity |
F | 0005524 | molecular_function | ATP binding |
F | 0006631 | biological_process | fatty acid metabolic process |
F | 0008610 | biological_process | lipid biosynthetic process |
F | 0008922 | molecular_function | long-chain fatty acid [acyl-carrier-protein] ligase activity |
F | 0016874 | molecular_function | ligase activity |
G | 0005524 | molecular_function | ATP binding |
G | 0006631 | biological_process | fatty acid metabolic process |
G | 0008610 | biological_process | lipid biosynthetic process |
G | 0008922 | molecular_function | long-chain fatty acid [acyl-carrier-protein] ligase activity |
G | 0016874 | molecular_function | ligase activity |
H | 0005524 | molecular_function | ATP binding |
H | 0006631 | biological_process | fatty acid metabolic process |
H | 0008610 | biological_process | lipid biosynthetic process |
H | 0008922 | molecular_function | long-chain fatty acid [acyl-carrier-protein] ligase activity |
H | 0016874 | molecular_function | ligase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | binding site for residue 5SV A 701 |
Chain | Residue |
A | HIS231 |
A | TYR343 |
A | GLY344 |
A | LEU345 |
A | ALA346 |
A | LEU350 |
A | ASP469 |
A | ILE480 |
A | ARG483 |
A | ASP232 |
A | THR237 |
A | ILE278 |
A | LEU311 |
A | SER314 |
A | GLU315 |
A | PRO316 |
A | SER342 |
site_id | AC2 |
Number of Residues | 13 |
Details | binding site for residue 5SV B 701 |
Chain | Residue |
B | HIS231 |
B | ASP232 |
B | THR237 |
B | SER314 |
B | PRO316 |
B | SER342 |
B | TYR343 |
B | GLY344 |
B | LEU345 |
B | ALA346 |
B | LEU350 |
B | ASP469 |
B | ARG483 |
site_id | AC3 |
Number of Residues | 16 |
Details | binding site for residue 5SV C 701 |
Chain | Residue |
C | HIS231 |
C | ASP232 |
C | MET233 |
C | THR237 |
C | LEU240 |
C | LEU311 |
C | SER314 |
C | GLU315 |
C | PRO316 |
C | SER342 |
C | TYR343 |
C | GLY344 |
C | LEU345 |
C | LEU350 |
C | ASP469 |
C | ARG483 |
site_id | AC4 |
Number of Residues | 15 |
Details | binding site for residue 5SV D 701 |
Chain | Residue |
D | GLY223 |
D | HIS231 |
D | ASP232 |
D | LEU311 |
D | SER314 |
D | GLU315 |
D | PRO316 |
D | SER342 |
D | TYR343 |
D | GLY344 |
D | ALA346 |
D | LEU350 |
D | ASP469 |
D | ARG483 |
D | LYS601 |
site_id | AC5 |
Number of Residues | 15 |
Details | binding site for residue 5SV E 701 |
Chain | Residue |
E | VAL211 |
E | HIS231 |
E | ASP232 |
E | THR237 |
E | LEU311 |
E | SER314 |
E | GLU315 |
E | PRO316 |
E | SER342 |
E | TYR343 |
E | GLY344 |
E | LEU345 |
E | LEU350 |
E | ASP469 |
E | ARG483 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue GOL E 702 |
Chain | Residue |
E | ALA386 |
E | VAL387 |
E | ALA388 |
E | TYR502 |
site_id | AC7 |
Number of Residues | 13 |
Details | binding site for residue 5SV F 701 |
Chain | Residue |
F | HIS231 |
F | ASP232 |
F | THR237 |
F | SER314 |
F | GLU315 |
F | PRO316 |
F | SER342 |
F | TYR343 |
F | GLY344 |
F | LEU345 |
F | LEU350 |
F | ASP469 |
F | ARG483 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue GOL F 702 |
Chain | Residue |
F | ALA386 |
F | ALA388 |
site_id | AC9 |
Number of Residues | 14 |
Details | binding site for residue 5SV G 701 |
Chain | Residue |
G | SER314 |
G | PRO316 |
G | ILE317 |
G | SER342 |
G | TYR343 |
G | GLY344 |
G | LEU345 |
G | LEU350 |
G | ASP469 |
G | ARG483 |
G | HIS231 |
G | ASP232 |
G | MET233 |
G | LEU311 |
site_id | AD1 |
Number of Residues | 14 |
Details | binding site for residue 5SV H 701 |
Chain | Residue |
H | HIS231 |
H | ASP232 |
H | THR237 |
H | VAL280 |
H | LEU311 |
H | SER314 |
H | ILE317 |
H | SER342 |
H | TYR343 |
H | GLY344 |
H | LEU345 |
H | ALA346 |
H | ASP469 |
H | ILE480 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 40 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26628098, ECO:0007744|PDB:5D6J |
Chain | Residue | Details |
A | THR187 | |
B | ARG483 | |
C | THR187 | |
C | SER342 | |
C | ALA346 | |
C | ASP469 | |
C | ARG483 | |
D | THR187 | |
D | SER342 | |
D | ALA346 | |
D | ASP469 | |
A | SER342 | |
D | ARG483 | |
E | THR187 | |
E | SER342 | |
E | ALA346 | |
E | ASP469 | |
E | ARG483 | |
F | THR187 | |
F | SER342 | |
F | ALA346 | |
F | ASP469 | |
A | ALA346 | |
F | ARG483 | |
G | THR187 | |
G | SER342 | |
G | ALA346 | |
G | ASP469 | |
G | ARG483 | |
H | THR187 | |
H | SER342 | |
H | ALA346 | |
H | ASP469 | |
A | ASP469 | |
H | ARG483 | |
A | ARG483 | |
B | THR187 | |
B | SER342 | |
B | ALA346 | |
B | ASP469 |