5NAG
Pseudomonas fluorescens kynurenine 3-monooxygenase (KMO) in complex with 3-{5-chloro-6-[(1R)-1-(pyridin-2-yl)ethoxy]-1,2-benzoxazol-3-yl}propanoic acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0004502 | molecular_function | kynurenine 3-monooxygenase activity |
| A | 0006569 | biological_process | tryptophan catabolic process |
| A | 0009435 | biological_process | NAD biosynthetic process |
| A | 0016174 | molecular_function | NAD(P)H oxidase H2O2-forming activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| A | 0019674 | biological_process | NAD metabolic process |
| A | 0019805 | biological_process | quinolinate biosynthetic process |
| A | 0034354 | biological_process | 'de novo' NAD biosynthetic process from tryptophan |
| A | 0043420 | biological_process | anthranilate metabolic process |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0070189 | biological_process | kynurenine metabolic process |
| A | 0071949 | molecular_function | FAD binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0004502 | molecular_function | kynurenine 3-monooxygenase activity |
| B | 0006569 | biological_process | tryptophan catabolic process |
| B | 0009435 | biological_process | NAD biosynthetic process |
| B | 0016174 | molecular_function | NAD(P)H oxidase H2O2-forming activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| B | 0019674 | biological_process | NAD metabolic process |
| B | 0019805 | biological_process | quinolinate biosynthetic process |
| B | 0034354 | biological_process | 'de novo' NAD biosynthetic process from tryptophan |
| B | 0043420 | biological_process | anthranilate metabolic process |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0070189 | biological_process | kynurenine metabolic process |
| B | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 38 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | ILE13 |
| A | LEU55 |
| A | ALA56 |
| A | ARG111 |
| A | GLY134 |
| A | LEU135 |
| A | ALA165 |
| A | ASP166 |
| A | GLY167 |
| A | ALA171 |
| A | TYR193 |
| A | GLY14 |
| A | GLU195 |
| A | GLY310 |
| A | ASP311 |
| A | GLY321 |
| A | GLN322 |
| A | GLY323 |
| A | MET324 |
| A | ASN325 |
| A | ALA327 |
| A | 8R5502 |
| A | GLY16 |
| A | HOH636 |
| A | HOH662 |
| A | HOH737 |
| A | HOH743 |
| A | HOH754 |
| A | HOH777 |
| A | HOH781 |
| A | HOH782 |
| A | HOH862 |
| A | LEU17 |
| A | ALA18 |
| A | GLU37 |
| A | ARG38 |
| A | ARG39 |
| A | ILE53 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue 8R5 A 502 |
| Chain | Residue |
| A | ALA56 |
| A | ARG84 |
| A | TYR98 |
| A | ILE224 |
| A | PHE238 |
| A | PRO318 |
| A | PHE319 |
| A | GLY321 |
| A | ASN369 |
| A | FAD501 |
| A | HOH706 |
| A | HOH801 |
| site_id | AC3 |
| Number of Residues | 38 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| B | ILE13 |
| B | GLY14 |
| B | GLY16 |
| B | LEU17 |
| B | ALA18 |
| B | GLU37 |
| B | ARG38 |
| B | ARG39 |
| B | LEU55 |
| B | ALA56 |
| B | ARG111 |
| B | GLY134 |
| B | LEU135 |
| B | ALA165 |
| B | ASP166 |
| B | GLY167 |
| B | ALA171 |
| B | GLU195 |
| B | GLY310 |
| B | ASP311 |
| B | GLY321 |
| B | GLN322 |
| B | GLY323 |
| B | MET324 |
| B | ASN325 |
| B | ALA327 |
| B | 8R5502 |
| B | HOH601 |
| B | HOH606 |
| B | HOH616 |
| B | HOH645 |
| B | HOH661 |
| B | HOH737 |
| B | HOH803 |
| B | HOH814 |
| B | HOH841 |
| B | HOH857 |
| B | HOH909 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | binding site for residue 8R5 B 502 |
| Chain | Residue |
| B | TYR404 |
| B | FAD501 |
| B | HOH601 |
| B | HOH604 |
| B | HOH622 |
| B | HOH739 |
| B | HOH836 |
| B | ALA56 |
| B | ARG84 |
| B | LEU213 |
| B | ILE215 |
| B | ILE224 |
| B | PHE238 |
| B | PRO318 |
| B | PHE319 |
| B | GLY321 |
| B | ASN369 |
| B | MET373 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28336141, ECO:0000269|PubMed:28398044, ECO:0000269|PubMed:28604669, ECO:0000269|PubMed:29208702, ECO:0000269|PubMed:29429898, ECO:0007744|PDB:5FN0, ECO:0007744|PDB:5MZC, ECO:0007744|PDB:5MZI, ECO:0007744|PDB:5MZK, ECO:0007744|PDB:5N7T, ECO:0007744|PDB:5NA5, ECO:0007744|PDB:5NAB, ECO:0007744|PDB:5NAE, ECO:0007744|PDB:5NAG, ECO:0007744|PDB:5NAH, ECO:0007744|PDB:5NAK, ECO:0007744|PDB:5X6P, ECO:0007744|PDB:5X6Q, ECO:0007744|PDB:5Y66, ECO:0007744|PDB:5Y77, ECO:0007744|PDB:5Y7A |
| Chain | Residue | Details |
| A | LEU17 | |
| B | ALA56 | |
| B | ARG111 | |
| B | LEU135 | |
| B | ASP311 | |
| B | MET324 | |
| A | GLU37 | |
| A | ALA56 | |
| A | ARG111 | |
| A | LEU135 | |
| A | ASP311 | |
| A | MET324 | |
| B | LEU17 | |
| B | GLU37 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29208702, ECO:0007744|PDB:5Y66, ECO:0007744|PDB:5Y77 |
| Chain | Residue | Details |
| A | ARG84 | |
| B | ARG84 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29208702, ECO:0007744|PDB:5Y77 |
| Chain | Residue | Details |
| A | TYR98 | |
| B | TYR98 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29208702, ECO:0007744|PDB:5Y66, ECO:0007744|PDB:5Y77, ECO:0007744|PDB:5Y7A |
| Chain | Residue | Details |
| A | ASN369 | |
| A | TYR404 | |
| B | ASN369 | |
| B | TYR404 |
