5VEP
MOUSE KYNURENINE AMINOTRANSFERASE III, RE-REFINEMENT OF THE PDB STRUCTURE 3E2F
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| A | 0006520 | biological_process | amino acid 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 | 0016829 | molecular_function | lyase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0047315 | molecular_function | kynurenine-glyoxylate 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 | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| B | 0006520 | biological_process | amino acid 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 | 0016829 | molecular_function | lyase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0047315 | molecular_function | kynurenine-glyoxylate 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 | 9 |
| Details | binding site for residue EPE A 501 |
| Chain | Residue |
| A | TRP54 |
| A | GLY72 |
| A | TYR136 |
| A | TYR160 |
| A | ASP161 |
| A | ASN219 |
| A | ARG430 |
| B | TYR312 |
| B | HOH640 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 502 |
| Chain | Residue |
| A | LEU179 |
| A | HIS424 |
| B | ARG199 |
| B | HOH611 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | ARG180 |
| A | SER181 |
| A | LYS182 |
| A | PHE196 |
| A | ASP197 |
| B | ARG180 |
| B | SER181 |
| B | LYS182 |
| B | THR195 |
| B | ASP197 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | GLN231 |
| A | ASP235 |
| A | VAL238 |
| A | PRO267 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | ASP241 |
| A | LEU243 |
| A | GLU271 |
| A | HIS298 |
| A | LEU299 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 506 |
| Chain | Residue |
| A | LYS182 |
| A | THR195 |
| A | THR226 |
| A | GLN228 |
| A | GLU229 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue CA A 507 |
| Chain | Residue |
| A | GLN122 |
| A | GLN122 |
| A | HOH645 |
| A | HOH645 |
| A | HOH659 |
| A | HOH672 |
| A | HOH672 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 508 |
| Chain | Residue |
| A | HIS240 |
| A | ASP241 |
| A | HOH622 |
| A | HOH664 |
| A | HOH665 |
| A | HOH668 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 509 |
| Chain | Residue |
| A | ASN42 |
| A | GLU47 |
| A | ASP437 |
| A | HOH602 |
| A | HOH612 |
| site_id | AD1 |
| Number of Residues | 13 |
| Details | binding site for residue EPE B 501 |
| Chain | Residue |
| A | GLN308 |
| A | TYR312 |
| B | ASN52 |
| B | TRP54 |
| B | GLN71 |
| B | GLY72 |
| B | TYR136 |
| B | TYR160 |
| B | ASP161 |
| B | ASN219 |
| B | ARG430 |
| B | HOH603 |
| B | HOH663 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue PEG B 502 |
| Chain | Residue |
| A | ASP197 |
| A | ARG199 |
| B | LEU179 |
| B | HIS424 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | GLN231 |
| B | ASP235 |
| B | PRO267 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | GLU251 |
| B | TRP252 |
| B | HOH604 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 505 |
| Chain | Residue |
| B | HIS240 |
| B | HOH639 |
| B | HOH647 |
| B | HOH668 |
| B | HOH673 |
| B | HOH687 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q16773","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"UniProtKB","id":"Q16773","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
