4WLJ
High resolution crystal structure of human kynurenine aminotransferase-I in complex with aminooxyacetate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016212 | molecular_function | L-kynurenine:2-oxoglutarate transaminase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0047316 | molecular_function | L-glutamine:phenylpyruvate transaminase activity |
| A | 0047804 | molecular_function | cysteine-S-conjugate beta-lyase activity |
| A | 0070189 | biological_process | kynurenine metabolic process |
| A | 0097053 | biological_process | L-kynurenine catabolic process |
| B | 0005515 | molecular_function | protein binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016212 | molecular_function | L-kynurenine:2-oxoglutarate transaminase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0047316 | molecular_function | L-glutamine:phenylpyruvate transaminase activity |
| B | 0047804 | molecular_function | cysteine-S-conjugate beta-lyase activity |
| B | 0070189 | biological_process | kynurenine metabolic process |
| B | 0097053 | biological_process | L-kynurenine catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue IK2 A 501 |
| Chain | Residue |
| A | GLY36 |
| A | TYR216 |
| A | SER244 |
| A | LYS247 |
| A | LYS255 |
| A | ARG398 |
| A | HOH646 |
| B | TYR63 |
| A | GLY99 |
| A | GLY100 |
| A | TYR101 |
| A | PHE125 |
| A | ASN181 |
| A | ASN185 |
| A | ASP213 |
| A | VAL215 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue IK2 B 501 |
| Chain | Residue |
| A | TYR63 |
| B | GLY36 |
| B | GLY99 |
| B | GLY100 |
| B | TYR101 |
| B | PHE125 |
| B | ASN181 |
| B | ASN185 |
| B | ASP213 |
| B | VAL215 |
| B | TYR216 |
| B | SER244 |
| B | LYS247 |
| B | LYS255 |
| B | ARG398 |
| B | HOH683 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15364907","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1W7M","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"15364907","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1W7L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1W7M","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
