3E9K
Crystal structure of Homo sapiens kynureninase-3-hydroxyhippuric acid inhibitor complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006569 | biological_process | tryptophan catabolic process |
| A | 0009435 | biological_process | NAD biosynthetic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| A | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
| A | 0019805 | biological_process | quinolinate biosynthetic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0030429 | molecular_function | kynureninase activity |
| A | 0034341 | biological_process | response to type II interferon |
| A | 0034354 | biological_process | 'de novo' NAD biosynthetic process from tryptophan |
| A | 0034516 | biological_process | response to vitamin B6 |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043420 | biological_process | anthranilate metabolic process |
| A | 0061981 | molecular_function | 3-hydroxykynureninase activity |
| A | 0097053 | biological_process | L-kynurenine catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP A 466 |
| Chain | Residue |
| A | LEU137 |
| A | TRP305 |
| A | SER332 |
| A | ASN333 |
| A | 3XH467 |
| A | HOH477 |
| A | HOH1099 |
| A | THR138 |
| A | PHE165 |
| A | ASP168 |
| A | ASP250 |
| A | ALA252 |
| A | HIS253 |
| A | TYR275 |
| A | LYS276 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 3XH A 467 |
| Chain | Residue |
| A | SER75 |
| A | HIS102 |
| A | PHE165 |
| A | HIS253 |
| A | TYR275 |
| A | LYS276 |
| A | TRP305 |
| A | ASN333 |
| A | ARG434 |
| A | PLP466 |
| A | HOH487 |
| A | HOH1092 |
| A | HOH1097 |
| A | HOH1099 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03017 |
| Chain | Residue | Details |
| A | LEU137 | |
| A | SER221 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03017, ECO:0000269|PubMed:17300176 |
| Chain | Residue | Details |
| A | THR138 | |
| A | ASP250 | |
| A | HIS253 | |
| A | TYR275 | |
| A | TRP305 | |
| A | ASN333 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | PHE165 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | MET1 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
| Chain | Residue | Details |
| A | LYS276 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cl1 |
| Chain | Residue | Details |
| A | PHE165 | |
| A | ASP250 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cl1 |
| Chain | Residue | Details |
| A | LYS276 | |
| A | PHE165 | |
| A | ASP250 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cl1 |
| Chain | Residue | Details |
| A | LYS276 | |
| A | HIS253 |
