5NAB
Pseudomonas fluorescens kynurenine 3-monooxygenase (KMO) in complex with 3-(5-chloro-6-methyl-2-oxo-2,3-dihydro-1,3-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 | 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 | 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 | ALA56 |
| A | ARG111 |
| A | GLY134 |
| A | LEU135 |
| A | ALA165 |
| A | ASP166 |
| A | GLY167 |
| A | ALA171 |
| A | GLY310 |
| A | ASP311 |
| A | GLY14 |
| A | GLY321 |
| A | GLN322 |
| A | GLY323 |
| A | MET324 |
| A | ASN325 |
| A | CL502 |
| A | 8RK503 |
| A | GOL504 |
| A | HOH651 |
| A | HOH661 |
| A | GLY16 |
| A | HOH662 |
| A | HOH668 |
| A | HOH705 |
| A | HOH735 |
| A | HOH810 |
| A | HOH818 |
| A | HOH820 |
| A | HOH837 |
| A | HOH863 |
| A | LEU17 |
| A | ALA18 |
| A | GLU37 |
| A | ARG38 |
| A | ARG39 |
| A | LEU55 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 502 |
| Chain | Residue |
| A | PRO318 |
| A | GLN322 |
| A | GLY323 |
| A | FAD501 |
| A | HOH882 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue 8RK A 503 |
| Chain | Residue |
| A | ALA56 |
| A | ARG84 |
| A | TYR98 |
| A | ILE106 |
| A | ILE224 |
| A | PHE238 |
| A | PRO318 |
| A | PHE319 |
| A | HIS320 |
| A | GLY321 |
| A | ASN369 |
| A | MET373 |
| A | TYR404 |
| A | FAD501 |
| A | HOH901 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | LEU292 |
| A | ALA293 |
| A | PRO315 |
| A | MET316 |
| A | FAD501 |
| A | HOH604 |
| A | HOH813 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | ARG84 |
| A | PRO97 |
| A | TYR98 |
| A | TYR404 |
| A | HOH701 |
| A | HOH865 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 506 |
| Chain | Residue |
| A | ARG28 |
| A | ASN29 |
| A | VAL332 |
| A | ALA335 |
| A | GLU336 |
| A | HOH666 |
| A | HOH684 |
| A | HOH734 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 507 |
| Chain | Residue |
| A | PRO42 |
| A | ILE44 |
| A | GLU45 |
| A | THR46 |
| A | ALA48 |
| A | GLY50 |
| A | HOH610 |
| site_id | AC8 |
| Number of Residues | 38 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| B | LEU135 |
| B | ALA165 |
| B | ASP166 |
| B | GLY167 |
| B | ALA171 |
| B | GLY310 |
| B | ASP311 |
| B | GLY321 |
| B | GLN322 |
| B | GLY323 |
| B | MET324 |
| B | ASN325 |
| B | CL502 |
| B | 8RK503 |
| B | GOL504 |
| B | GOL505 |
| B | HOH619 |
| B | HOH647 |
| B | HOH648 |
| B | HOH676 |
| B | HOH696 |
| B | HOH745 |
| B | HOH759 |
| B | HOH806 |
| B | HOH915 |
| B | ILE13 |
| B | GLY14 |
| B | GLY16 |
| B | LEU17 |
| B | ALA18 |
| B | GLU37 |
| B | ARG38 |
| B | ARG39 |
| B | ILE53 |
| B | LEU55 |
| B | ALA56 |
| B | ARG111 |
| B | GLY134 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 502 |
| Chain | Residue |
| B | PRO318 |
| B | GLN322 |
| B | GLY323 |
| B | FAD501 |
| site_id | AD1 |
| Number of Residues | 16 |
| Details | binding site for residue 8RK B 503 |
| Chain | Residue |
| B | ALA56 |
| B | ARG84 |
| B | ILE224 |
| B | PHE238 |
| B | PRO318 |
| B | PHE319 |
| B | HIS320 |
| B | GLY321 |
| B | ASN369 |
| B | MET373 |
| B | TYR404 |
| B | FAD501 |
| B | GOL506 |
| B | HOH622 |
| B | HOH651 |
| B | HOH812 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | LEU17 |
| B | ARG39 |
| B | ARG111 |
| B | ASN115 |
| B | FAD501 |
| B | HOH785 |
| B | HOH865 |
| site_id | AD3 |
| Number of Residues | 10 |
| Details | binding site for residue GOL B 505 |
| Chain | Residue |
| B | CYS168 |
| B | LEU292 |
| B | ALA293 |
| B | PRO315 |
| B | MET316 |
| B | VAL317 |
| B | FAD501 |
| B | HOH645 |
| B | HOH848 |
| B | HOH927 |
| site_id | AD4 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 506 |
| Chain | Residue |
| B | ARG84 |
| B | GLN96 |
| B | PRO97 |
| B | TYR98 |
| B | ARG386 |
| B | TYR404 |
| B | 8RK503 |
| B | HOH615 |
| B | HOH932 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 507 |
| Chain | Residue |
| B | LEU25 |
| B | ARG28 |
| B | ASN29 |
| B | VAL332 |
| B | ALA335 |
| B | GLU336 |
| B | HOH935 |
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 |
