2XH1
Crystal structure of human KAT II-inhibitor complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| A | 0006536 | biological_process | glutamate metabolic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016212 | molecular_function | kynurenine-oxoglutarate transaminase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0033512 | biological_process | L-lysine catabolic process to acetyl-CoA via L-saccharopine |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0047315 | molecular_function | kynurenine-glyoxylate transaminase activity |
| A | 0047536 | molecular_function | 2-aminoadipate transaminase activity |
| A | 0047958 | molecular_function | glycine:2-oxoglutarate aminotransferase activity |
| A | 0050094 | molecular_function | methionine-glyoxylate transaminase activity |
| A | 0070189 | biological_process | kynurenine metabolic process |
| A | 1901605 | biological_process | alpha-amino acid metabolic process |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| B | 0006536 | biological_process | glutamate metabolic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016212 | molecular_function | kynurenine-oxoglutarate transaminase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0033512 | biological_process | L-lysine catabolic process to acetyl-CoA via L-saccharopine |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0047315 | molecular_function | kynurenine-glyoxylate transaminase activity |
| B | 0047536 | molecular_function | 2-aminoadipate transaminase activity |
| B | 0047958 | molecular_function | glycine:2-oxoglutarate aminotransferase activity |
| B | 0050094 | molecular_function | methionine-glyoxylate transaminase activity |
| B | 0070189 | biological_process | kynurenine metabolic process |
| B | 1901605 | biological_process | alpha-amino acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BF5 A 1426 |
| Chain | Residue |
| A | TYR142 |
| A | PLP1427 |
| A | HOH2240 |
| A | HOH2241 |
| B | GLY39 |
| B | LEU40 |
| B | SER75 |
| B | PRO76 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP A 1427 |
| Chain | Residue |
| A | GLN118 |
| A | TYR142 |
| A | ASN202 |
| A | ASP230 |
| A | PRO232 |
| A | TYR233 |
| A | SER260 |
| A | SER262 |
| A | LYS263 |
| A | ARG270 |
| A | BF51426 |
| A | HOH2187 |
| B | TYR74 |
| A | SER117 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BF5 B 1426 |
| Chain | Residue |
| A | GLY39 |
| A | LEU40 |
| A | TYR74 |
| A | SER77 |
| B | TYR142 |
| B | PLP1427 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP B 1427 |
| Chain | Residue |
| A | TYR74 |
| B | SER117 |
| B | GLN118 |
| B | TYR142 |
| B | ASN202 |
| B | ASP230 |
| B | PRO232 |
| B | TYR233 |
| B | SER260 |
| B | SER262 |
| B | LYS263 |
| B | ARG270 |
| B | BF51426 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IOD A 1428 |
| Chain | Residue |
| A | GLN119 |
| A | LYS123 |
| B | GLN119 |
| B | LYS123 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1428 |
| Chain | Residue |
| B | GLU-1 |
| B | ASN2 |
| B | SER105 |
| B | PRO279 |
| B | HOH2173 |
| B | HOH2174 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 54 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9WVM8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9WVM8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
