5XDC
Crystal structure of Indole-bound TdsC from Paenibacillus sp. A11-2
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006552 | biological_process | L-leucine catabolic process |
A | 0008470 | molecular_function | isovaleryl-CoA dehydrogenase activity |
A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004497 | molecular_function | monooxygenase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006552 | biological_process | L-leucine catabolic process |
B | 0008470 | molecular_function | isovaleryl-CoA dehydrogenase activity |
B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0004497 | molecular_function | monooxygenase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0006552 | biological_process | L-leucine catabolic process |
C | 0008470 | molecular_function | isovaleryl-CoA dehydrogenase activity |
C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0004497 | molecular_function | monooxygenase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0006552 | biological_process | L-leucine catabolic process |
D | 0008470 | molecular_function | isovaleryl-CoA dehydrogenase activity |
D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue IND A 501 |
Chain | Residue |
A | HIS89 |
A | PHE158 |
A | SER160 |
A | SER212 |
A | THR384 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue SO4 A 502 |
Chain | Residue |
A | HOH753 |
C | ASN179 |
C | ARG183 |
C | THR230 |
A | ARG63 |
A | LYS110 |
A | HOH603 |
A | HOH615 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 503 |
Chain | Residue |
A | ARG319 |
A | ARG326 |
A | GLN333 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 504 |
Chain | Residue |
A | ARG279 |
A | GLY364 |
A | ALA365 |
A | ARG366 |
A | HOH608 |
B | ASN132 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 505 |
Chain | Residue |
A | ARG326 |
A | ASN327 |
A | HIS328 |
site_id | AC6 |
Number of Residues | 8 |
Details | binding site for residue IND B 501 |
Chain | Residue |
B | HIS89 |
B | GLU130 |
B | PHE158 |
B | SER160 |
B | THR210 |
B | SER212 |
B | THR384 |
B | HIS388 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 502 |
Chain | Residue |
B | ARG319 |
B | ARG326 |
B | GLN333 |
B | HOH641 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 503 |
Chain | Residue |
B | HIS272 |
B | ARG275 |
B | HOH666 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue GOL B 504 |
Chain | Residue |
B | GLN109 |
B | ARG112 |
B | TRP113 |
B | ASP225 |
B | HOH631 |
B | HOH643 |
B | HOH653 |
B | HOH734 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 505 |
Chain | Residue |
B | ARG326 |
B | ASN327 |
B | HIS328 |
B | HOH788 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue SO4 C 501 |
Chain | Residue |
B | GLU291 |
C | ARG396 |
C | ASN400 |
C | ARG406 |
site_id | AD3 |
Number of Residues | 9 |
Details | binding site for residue IND C 502 |
Chain | Residue |
C | HIS89 |
C | TYR93 |
C | GLU130 |
C | PHE158 |
C | SER160 |
C | SER212 |
C | THR384 |
C | HIS388 |
D | ALA365 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue SO4 C 503 |
Chain | Residue |
C | ARG319 |
C | ARG326 |
C | GLN333 |
C | HOH726 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue SO4 C 504 |
Chain | Residue |
C | ARG326 |
C | ASN327 |
C | HIS328 |
C | HOH608 |
C | HOH736 |
C | HOH803 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue SO4 C 505 |
Chain | Residue |
C | HIS272 |
C | ARG275 |
C | HOH634 |
site_id | AD7 |
Number of Residues | 7 |
Details | binding site for residue GOL C 506 |
Chain | Residue |
C | ARG112 |
C | TRP113 |
C | ASP225 |
C | HOH638 |
C | HOH732 |
C | HOH738 |
C | HOH769 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue SO4 C 507 |
Chain | Residue |
C | ARG279 |
C | GLY364 |
C | ALA365 |
C | ARG366 |
C | HOH637 |
C | HOH764 |
site_id | AD9 |
Number of Residues | 8 |
Details | binding site for residue IND D 501 |
Chain | Residue |
C | ALA365 |
D | HIS89 |
D | PHE158 |
D | SER160 |
D | SER212 |
D | THR384 |
D | HIS385 |
D | HIS388 |
site_id | AE1 |
Number of Residues | 6 |
Details | binding site for residue SO4 D 502 |
Chain | Residue |
D | ARG319 |
D | ARG326 |
D | GLN333 |
D | HOH723 |
D | HOH837 |
D | HOH897 |
site_id | AE2 |
Number of Residues | 7 |
Details | binding site for residue GOL D 503 |
Chain | Residue |
D | ARG112 |
D | TRP113 |
D | ASP225 |
D | HOH628 |
D | HOH649 |
D | HOH745 |
D | HOH805 |
site_id | AE3 |
Number of Residues | 5 |
Details | binding site for residue SO4 D 504 |
Chain | Residue |
D | HIS272 |
D | ARG275 |
D | HOH612 |
D | HOH633 |
D | HOH653 |
site_id | AE4 |
Number of Residues | 3 |
Details | binding site for residue SO4 D 505 |
Chain | Residue |
D | ARG326 |
D | ASN327 |
D | HIS328 |
site_id | AE5 |
Number of Residues | 7 |
Details | binding site for residue SO4 D 506 |
Chain | Residue |
D | ARG279 |
D | GLY364 |
D | ALA365 |
D | ARG366 |
D | HOH609 |
D | HOH657 |
D | HOH890 |