5VEQ
MOUSE KYNURENINE AMINOTRANSFERASE III, RE-REFINEMENT OF THE PDB STRUCTURE 3E2Y
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 | 15 |
Details | binding site for residue PMP A 501 |
Chain | Residue |
A | GLY134 |
A | LYS281 |
A | LYS289 |
A | EPE502 |
A | HOH654 |
A | HOH690 |
B | TYR98 |
A | ALA135 |
A | TYR136 |
A | TYR160 |
A | ASN215 |
A | ASN219 |
A | ASP247 |
A | TYR250 |
A | SER278 |
site_id | AC2 |
Number of Residues | 14 |
Details | binding site for residue EPE A 502 |
Chain | Residue |
A | TRP54 |
A | GLY72 |
A | TYR160 |
A | ASN219 |
A | PHE373 |
A | ARG430 |
A | PMP501 |
A | HOH654 |
A | HOH698 |
B | TYR98 |
B | THR99 |
B | GLY101 |
B | TYR312 |
B | THR313 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue PGE A 503 |
Chain | Residue |
A | LEU179 |
A | HIS424 |
A | PHE425 |
B | ARG199 |
B | HOH617 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue GOL A 504 |
Chain | Residue |
A | MET156 |
A | PRO158 |
A | PHE159 |
A | TYR160 |
A | TYR163 |
A | ASN215 |
A | HIS218 |
A | ASN219 |
A | TYR225 |
A | HOH610 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue GOL A 505 |
Chain | Residue |
A | LYS182 |
A | SER192 |
A | THR195 |
A | THR226 |
A | GLU229 |
A | HOH620 |
site_id | AC6 |
Number of Residues | 8 |
Details | binding site for residue CA A 506 |
Chain | Residue |
A | GLN122 |
A | GLN122 |
A | HOH643 |
A | HOH643 |
A | HOH648 |
A | HOH648 |
A | HOH814 |
A | HOH814 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue CA A 507 |
Chain | Residue |
A | HIS240 |
A | HOH615 |
A | HOH657 |
A | HOH659 |
A | HOH714 |
A | HOH794 |
A | HOH797 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue CA A 508 |
Chain | Residue |
A | ASN42 |
A | GLU47 |
A | HOH609 |
A | HOH711 |
A | HOH741 |
A | HOH774 |
A | HOH807 |
site_id | AC9 |
Number of Residues | 14 |
Details | binding site for residue PMP B 501 |
Chain | Residue |
A | TYR98 |
B | GLY134 |
B | ALA135 |
B | TYR136 |
B | ASN215 |
B | ASN219 |
B | ASP247 |
B | TYR250 |
B | SER278 |
B | LYS281 |
B | LYS289 |
B | EPE502 |
B | HOH624 |
B | HOH658 |
site_id | AD1 |
Number of Residues | 15 |
Details | binding site for residue EPE B 502 |
Chain | Residue |
B | HOH645 |
B | HOH658 |
A | TYR98 |
A | THR99 |
A | GLY101 |
A | TYR312 |
A | THR313 |
B | TRP54 |
B | GLN71 |
B | GLY72 |
B | TYR160 |
B | ASN219 |
B | PHE373 |
B | ARG430 |
B | PMP501 |
site_id | AD2 |
Number of Residues | 9 |
Details | binding site for residue PG4 B 503 |
Chain | Residue |
A | ASP197 |
A | ARG199 |
A | GLU200 |
B | LEU179 |
B | ARG180 |
B | SER181 |
B | TRP194 |
B | PRO423 |
B | HIS424 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue GOL B 504 |
Chain | Residue |
B | GLN231 |
B | ASP235 |
B | PRO267 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue GOL B 505 |
Chain | Residue |
B | GLU251 |
B | TRP252 |
B | HIS260 |
B | LYS262 |
B | HOH646 |
site_id | AD5 |
Number of Residues | 7 |
Details | binding site for residue CA B 506 |
Chain | Residue |
B | HIS240 |
B | HOH632 |
B | HOH643 |
B | HOH698 |
B | HOH726 |
B | HOH758 |
B | HOH777 |
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 |