6FOZ
The crystal structure of P.fluorescens Kynurenine 3-monooxygenase (KMO) in complex with competitive inhibitor No. 13
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 | 34 |
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 | GLU194 |
A | GLY13 |
A | GLY309 |
A | ASP310 |
A | GLY320 |
A | GLN321 |
A | GLY322 |
A | MET323 |
A | ASN324 |
A | E0H502 |
A | HOH603 |
A | HOH606 |
A | GLY15 |
A | HOH610 |
A | HOH631 |
A | HOH632 |
A | HOH637 |
A | HOH684 |
A | LEU16 |
A | ALA17 |
A | GLU36 |
A | ARG37 |
A | ARG38 |
A | LEU54 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue E0H A 502 |
Chain | Residue |
A | ALA55 |
A | ARG83 |
A | TYR97 |
A | LEU212 |
A | ILE223 |
A | PHE237 |
A | PRO317 |
A | PHE318 |
A | GLY320 |
A | FAD501 |
A | HOH633 |
site_id | AC3 |
Number of Residues | 32 |
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 | TYR192 |
B | GLU194 |
B | GLY309 |
B | ASP310 |
B | GLY320 |
B | GLN321 |
B | GLY322 |
B | MET323 |
B | ASN324 |
B | E0H502 |
B | HOH616 |
B | HOH619 |
B | HOH623 |
B | HOH624 |
B | HOH656 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue E0H B 502 |
Chain | Residue |
B | ALA55 |
B | ARG83 |
B | TYR97 |
B | LEU212 |
B | ILE223 |
B | PHE237 |
B | PRO317 |
B | PHE318 |
B | GLY320 |
B | FAD501 |
B | HOH608 |
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 | MET323 | |
B | LEU16 | |
B | GLU36 | |
B | ALA55 | |
B | ARG110 | |
B | LEU134 | |
B | ASP310 | |
B | MET323 | |
A | LEU16 | |
A | GLU36 | |
A | ALA55 | |
A | ARG110 | |
A | LEU134 | |
A | ASP310 |
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 |
B | ASN368 | |
B | TYR403 | |
A | ASN368 | |
A | TYR403 |