5TKQ
Crystal structure of human 3HAO with zinc bound in the active site
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000334 | molecular_function | 3-hydroxyanthranilate 3,4-dioxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006569 | biological_process | L-tryptophan catabolic process |
| A | 0008198 | molecular_function | ferrous iron binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0009435 | biological_process | NAD+ biosynthetic process |
| A | 0010043 | biological_process | response to zinc ion |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| A | 0019805 | biological_process | quinolinate biosynthetic process |
| A | 0034354 | biological_process | 'de novo' NAD+ biosynthetic process from L-tryptophan |
| A | 0043420 | biological_process | anthranilate metabolic process |
| A | 0043648 | biological_process | dicarboxylic acid metabolic process |
| A | 0046686 | biological_process | response to cadmium ion |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046874 | biological_process | quinolinate metabolic process |
| A | 0051213 | molecular_function | dioxygenase activity |
| A | 0070050 | biological_process | neuron cellular homeostasis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | HIS47 |
| A | GLU53 |
| A | HIS91 |
| A | HOH491 |
| A | HOH544 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 302 |
| Chain | Residue |
| A | HOH439 |
| A | ARG88 |
| A | SER173 |
| A | THR174 |
| A | ARG175 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 303 |
| Chain | Residue |
| A | ARG175 |
| A | SER176 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 304 |
| Chain | Residue |
| A | CYS23 |
| A | ASN24 |
| A | ILE37 |
| A | ASN41 |
| A | ARG43 |
| A | HOH436 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 305 |
| Chain | Residue |
| A | ARG223 |
| A | THR260 |
| A | SER261 |
| A | HOH447 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 306 |
| Chain | Residue |
| A | ARG8 |
| A | TYR56 |
| A | TRP231 |
| A | GLU234 |
| A | ASP251 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Region: {"description":"Linker","evidences":[{"source":"HAMAP-Rule","id":"MF_03019","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03019","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03019","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28375145","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5TK5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
