6FPH
The crystal structure of P.fluorescens Kynurenine 3-monooxygenase (KMO) in complex with competitive inhibitor No. 1h
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 | 36 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | ILE12 |
| A | ALA55 |
| A | ARG110 |
| A | GLY133 |
| A | LEU134 |
| A | ALA164 |
| A | ASP165 |
| A | GLY166 |
| A | ALA170 |
| A | TYR192 |
| A | GLY309 |
| A | GLY13 |
| A | ASP310 |
| A | GLY320 |
| A | GLN321 |
| A | GLY322 |
| A | MET323 |
| A | ASN324 |
| A | CL502 |
| A | E1W503 |
| A | HOH627 |
| A | HOH631 |
| A | GLY15 |
| A | HOH658 |
| A | HOH660 |
| A | HOH667 |
| A | HOH685 |
| A | HOH717 |
| A | HOH759 |
| A | HOH777 |
| A | LEU16 |
| A | ALA17 |
| A | GLU36 |
| A | ARG37 |
| A | ARG38 |
| A | LEU54 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 502 |
| Chain | Residue |
| A | PRO317 |
| A | GLN321 |
| A | GLY322 |
| A | FAD501 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue E1W A 503 |
| Chain | Residue |
| A | ALA55 |
| A | ARG83 |
| A | TYR97 |
| A | LEU212 |
| A | ILE223 |
| A | PRO317 |
| A | PHE318 |
| A | GLY320 |
| A | ASN368 |
| A | MET372 |
| A | TYR403 |
| A | FAD501 |
| site_id | AC4 |
| Number of Residues | 34 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| B | ILE12 |
| B | GLY13 |
| B | GLY15 |
| B | LEU16 |
| B | ALA17 |
| B | GLU36 |
| B | ARG37 |
| B | ARG38 |
| B | LEU54 |
| B | ALA55 |
| B | ARG110 |
| B | GLY133 |
| B | LEU134 |
| B | ALA164 |
| B | ASP165 |
| B | GLY166 |
| B | ALA170 |
| B | GLY309 |
| B | ASP310 |
| B | GLY320 |
| B | GLN321 |
| B | GLY322 |
| B | MET323 |
| B | ASN324 |
| B | CL502 |
| B | E1W503 |
| B | HOH612 |
| B | HOH616 |
| B | HOH636 |
| B | HOH647 |
| B | HOH700 |
| B | HOH712 |
| B | HOH716 |
| B | HOH754 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 502 |
| Chain | Residue |
| B | PRO317 |
| B | GLN321 |
| B | GLY322 |
| B | FAD501 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue E1W B 503 |
| Chain | Residue |
| B | ASN368 |
| B | MET372 |
| B | TYR403 |
| B | FAD501 |
| B | HOH603 |
| B | ALA55 |
| B | ARG83 |
| B | LEU212 |
| B | ILE214 |
| B | ILE223 |
| B | PHE237 |
| B | PRO317 |
| B | PHE318 |
| B | GLY320 |
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 | LEU16 | |
| B | ALA55 | |
| B | ARG110 | |
| B | LEU134 | |
| B | ASP310 | |
| B | MET323 | |
| A | GLU36 | |
| A | ALA55 | |
| A | ARG110 | |
| A | LEU134 | |
| A | ASP310 | |
| A | MET323 | |
| B | LEU16 | |
| B | GLU36 |
| 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 | ARG83 | |
| B | ARG83 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29208702, ECO:0007744|PDB:5Y77 |
| Chain | Residue | Details |
| A | TYR97 | |
| B | TYR97 |
| 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 | ASN368 | |
| A | TYR403 | |
| B | ASN368 | |
| B | TYR403 |
