4PXO
Crystal structure of Maleylacetoacetate isomerase from Methylobacteriu extorquens AM1 WITH BOUND MALONATE AND GSH (TARGET EFI-507068)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004364 | molecular_function | glutathione transferase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006559 | biological_process | L-phenylalanine catabolic process |
A | 0006749 | biological_process | glutathione metabolic process |
A | 0009072 | biological_process | aromatic amino acid metabolic process |
A | 0016034 | molecular_function | maleylacetoacetate isomerase activity |
A | 0016740 | molecular_function | transferase activity |
A | 0016853 | molecular_function | isomerase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0004364 | molecular_function | glutathione transferase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006559 | biological_process | L-phenylalanine catabolic process |
B | 0006749 | biological_process | glutathione metabolic process |
B | 0009072 | biological_process | aromatic amino acid metabolic process |
B | 0016034 | molecular_function | maleylacetoacetate isomerase activity |
B | 0016740 | molecular_function | transferase activity |
B | 0016853 | molecular_function | isomerase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MLA A 301 |
Chain | Residue |
A | ARG8 |
A | ALA10 |
A | HIS105 |
A | PRO110 |
A | ARG113 |
A | GSH302 |
A | EDO304 |
A | HOH459 |
site_id | AC2 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE GSH A 302 |
Chain | Residue |
A | ALA10 |
A | ALA11 |
A | ARG14 |
A | LEU33 |
A | GLN38 |
A | ALA51 |
A | VAL52 |
A | PRO53 |
A | GLN65 |
A | SER66 |
A | HIS105 |
A | PRO110 |
A | ARG111 |
A | MLA301 |
A | HOH415 |
A | HOH420 |
A | HOH435 |
A | HOH455 |
A | HOH594 |
B | CYS102 |
B | ASP103 |
A | SER9 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 303 |
Chain | Residue |
A | ARG154 |
A | ARG154 |
A | GLU194 |
A | ALA197 |
A | LEU198 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 304 |
Chain | Residue |
A | ARG8 |
A | ALA10 |
A | SER170 |
A | VAL173 |
A | ILE177 |
A | PHE178 |
A | MLA301 |
A | HOH413 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 305 |
Chain | Residue |
A | TRP7 |
A | TYR72 |
A | PRO213 |
B | GLU86 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MLA B 301 |
Chain | Residue |
B | ARG8 |
B | ALA10 |
B | HIS105 |
B | ARG113 |
B | GSH302 |
B | EDO307 |
B | HOH472 |
site_id | AC7 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE GSH B 302 |
Chain | Residue |
A | CYS102 |
A | ASP103 |
A | HOH443 |
B | SER9 |
B | ALA10 |
B | ALA11 |
B | ARG14 |
B | LEU33 |
B | GLN38 |
B | GLY50 |
B | ALA51 |
B | VAL52 |
B | PRO53 |
B | GLN65 |
B | SER66 |
B | HIS105 |
B | VAL109 |
B | PRO110 |
B | ARG111 |
B | MLA301 |
B | EDO304 |
B | HOH406 |
B | HOH414 |
B | HOH426 |
B | HOH533 |
B | HOH535 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 303 |
Chain | Residue |
A | LEU107 |
A | PHE130 |
A | ASN133 |
A | ALA134 |
B | ARG111 |
B | VAL112 |
B | PHE115 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 304 |
Chain | Residue |
A | HOH539 |
B | GLN49 |
B | VAL109 |
B | ARG111 |
B | GSH302 |
B | HOH422 |
B | HOH534 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 305 |
Chain | Residue |
B | HOH556 |
A | PHE115 |
B | PHE130 |
B | ASN133 |
B | ALA134 |
B | HOH519 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 306 |
Chain | Residue |
B | ASN20 |
B | ALA200 |
B | HOH438 |
B | HOH489 |
B | HOH563 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 307 |
Chain | Residue |
B | ARG8 |
B | ALA10 |
B | TYR108 |
B | ILE177 |
B | MLA301 |
B | HOH413 |