5MZK
Pseudomonas fluorescens kynurenine 3-monooxygenase (KMO) in complex with 3-[5-chloro-6-(cyclobutylmethoxy)-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 | L-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 | 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 | L-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 | 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 | 36 |
| 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 | PRO318 |
| A | GLY321 |
| A | GLN322 |
| A | GLY323 |
| A | MET324 |
| A | ASN325 |
| A | CL502 |
| A | OK1503 |
| A | HOH608 |
| A | HOH633 |
| A | GLY16 |
| A | HOH636 |
| A | HOH654 |
| A | HOH664 |
| A | HOH713 |
| A | HOH728 |
| A | HOH738 |
| A | HOH777 |
| 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 | HOH762 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | binding site for residue OK1 A 503 |
| Chain | Residue |
| A | ASN54 |
| A | ALA56 |
| A | ARG84 |
| A | TYR98 |
| A | ILE106 |
| A | ILE224 |
| A | THR236 |
| A | PRO318 |
| A | PHE319 |
| A | HIS320 |
| A | GLY321 |
| A | ASN369 |
| A | MET373 |
| A | TYR404 |
| A | FAD501 |
| A | HOH820 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue OK1 A 504 |
| Chain | Residue |
| A | LEU427 |
| A | PHE430 |
| A | ALA431 |
| A | HIS435 |
| A | ILE441 |
| A | ASN442 |
| A | ALA445 |
| A | GLU449 |
| A | HOH630 |
| B | ARG296 |
| B | MET418 |
| B | HOH657 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | LEU292 |
| A | ALA293 |
| A | ASP311 |
| A | PRO315 |
| A | MET316 |
| A | HOH633 |
| A | HOH662 |
| site_id | AC6 |
| Number of Residues | 40 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| B | MET324 |
| B | ASN325 |
| B | ALA327 |
| B | CL502 |
| B | OK1503 |
| B | GOL504 |
| B | HOH608 |
| B | HOH623 |
| B | HOH641 |
| B | HOH660 |
| B | HOH666 |
| B | HOH683 |
| B | HOH720 |
| B | HOH763 |
| B | HOH773 |
| B | HOH815 |
| B | HOH848 |
| 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 |
| B | LEU135 |
| B | ALA165 |
| B | ASP166 |
| B | GLY167 |
| B | ALA171 |
| B | GLY310 |
| B | ASP311 |
| B | GLY321 |
| B | GLN322 |
| B | GLY323 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue CL B 502 |
| Chain | Residue |
| B | PRO318 |
| B | GLN322 |
| B | GLY323 |
| B | FAD501 |
| B | HOH623 |
| B | HOH843 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | binding site for residue OK1 B 503 |
| Chain | Residue |
| B | ALA56 |
| B | ARG84 |
| B | ILE106 |
| B | ILE215 |
| B | ILE224 |
| B | THR236 |
| B | PHE238 |
| B | PRO318 |
| B | PHE319 |
| B | HIS320 |
| B | GLY321 |
| B | ASN369 |
| B | MET373 |
| B | TYR404 |
| B | FAD501 |
| B | HOH601 |
| B | HOH612 |
| B | HOH737 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | CYS168 |
| B | LEU292 |
| B | ALA293 |
| B | PRO315 |
| B | MET316 |
| B | VAL317 |
| B | FAD501 |
| B | HOH703 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28336141","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28398044","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28604669","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29208702","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29429898","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5FN0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MZC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MZI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MZK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5N7T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NA5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NAB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NAE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NAG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NAH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NAK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5X6P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5X6Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5Y66","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5Y77","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5Y7A","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29208702","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5Y66","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5Y77","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29208702","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5Y77","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29208702","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5Y66","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5Y77","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5Y7A","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
