3KGW
Crystal structure of Putative aminotransferase (AAH25799.1) from MUS MUSCULUS at 1.65 A resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004760 | molecular_function | serine-pyruvate transaminase activity |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0005777 | cellular_component | peroxisome |
A | 0005782 | cellular_component | peroxisomal matrix |
A | 0006563 | biological_process | L-serine metabolic process |
A | 0007219 | biological_process | Notch signaling pathway |
A | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
A | 0008483 | molecular_function | transaminase activity |
A | 0009436 | biological_process | glyoxylate catabolic process |
A | 0016597 | molecular_function | amino acid binding |
A | 0019265 | biological_process | glycine biosynthetic process, by transamination of glyoxylate |
A | 0019448 | biological_process | L-cysteine catabolic process |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0042853 | biological_process | L-alanine catabolic process |
A | 0042866 | biological_process | pyruvate biosynthetic process |
A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
A | 0043621 | molecular_function | obsolete protein self-association |
A | 0046487 | biological_process | glyoxylate metabolic process |
A | 0046724 | biological_process | oxalic acid secretion |
A | 0051384 | biological_process | response to glucocorticoid |
A | 0051591 | biological_process | response to cAMP |
B | 0004760 | molecular_function | serine-pyruvate transaminase activity |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0005777 | cellular_component | peroxisome |
B | 0005782 | cellular_component | peroxisomal matrix |
B | 0006563 | biological_process | L-serine metabolic process |
B | 0007219 | biological_process | Notch signaling pathway |
B | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
B | 0008483 | molecular_function | transaminase activity |
B | 0009436 | biological_process | glyoxylate catabolic process |
B | 0016597 | molecular_function | amino acid binding |
B | 0019265 | biological_process | glycine biosynthetic process, by transamination of glyoxylate |
B | 0019448 | biological_process | L-cysteine catabolic process |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0042802 | molecular_function | identical protein binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0042853 | biological_process | L-alanine catabolic process |
B | 0042866 | biological_process | pyruvate biosynthetic process |
B | 0043231 | cellular_component | intracellular membrane-bounded organelle |
B | 0043621 | molecular_function | obsolete protein self-association |
B | 0046487 | biological_process | glyoxylate metabolic process |
B | 0046724 | biological_process | oxalic acid secretion |
B | 0051384 | biological_process | response to glucocorticoid |
B | 0051591 | biological_process | response to cAMP |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PLP A 500 |
Chain | Residue |
A | SER103 |
A | GLN230 |
A | LYS231 |
B | THR285 |
A | GLY104 |
A | HIS105 |
A | TRP130 |
A | GLY178 |
A | SER180 |
A | ASP205 |
A | VAL207 |
A | SER228 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 502 |
Chain | Residue |
A | ASN54 |
A | LEU55 |
B | MET67 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 503 |
Chain | Residue |
A | GLU315 |
A | THR392 |
A | HOH792 |
B | HOH780 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 504 |
Chain | Residue |
A | PHE113 |
A | LEU116 |
A | PRO118 |
A | ILE141 |
A | ARG255 |
A | PRO259 |
A | VAL260 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 506 |
Chain | Residue |
A | ARG93 |
A | PRO95 |
A | VAL145 |
A | ASP246 |
A | HOH602 |
A | HOH709 |
A | HOH868 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 507 |
Chain | Residue |
A | PRO187 |
A | LEU188 |
A | ASP189 |
A | HOH643 |
A | HOH854 |
A | HOH875 |
site_id | AC7 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PLP B 500 |
Chain | Residue |
A | THR285 |
B | SER103 |
B | GLY104 |
B | HIS105 |
B | TRP130 |
B | GLY178 |
B | SER180 |
B | ASP205 |
B | VAL207 |
B | SER228 |
B | GLN230 |
B | LYS231 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL B 501 |
Chain | Residue |
A | ARG66 |
A | MET67 |
B | ASN54 |
B | LEU55 |
B | HOH814 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 505 |
Chain | Residue |
B | PHE113 |
B | LEU116 |
B | GLU117 |
B | ILE141 |
B | ARG255 |
B | PRO259 |
B | VAL260 |
Functional Information from PROSITE/UniProt
site_id | PS00595 |
Number of Residues | 21 |
Details | AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. IDIMysSSQKvlnappGiSlI |
Chain | Residue | Details |
A | ILE222-ILE242 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ARG382 | |
B | ARG382 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
Chain | Residue | Details |
A | LYS231 | |
B | LYS231 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 |
Chain | Residue | Details |
A | LYS247 | |
A | LYS330 | |
B | LYS247 | |
B | LYS330 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23576753 |
Chain | Residue | Details |
A | LYS256 | |
A | LYS334 | |
B | LYS256 | |
B | LYS334 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b8g |
Chain | Residue | Details |
A | LYS231 | |
A | TRP130 | |
A | ASP205 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b8g |
Chain | Residue | Details |
B | LYS231 | |
B | TRP130 | |
B | ASP205 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b8g |
Chain | Residue | Details |
A | LYS251 | |
A | TRP130 | |
A | ASP205 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b8g |
Chain | Residue | Details |
B | LYS251 | |
B | TRP130 | |
B | ASP205 |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1b8g |
Chain | Residue | Details |
A | LYS73 |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1b8g |
Chain | Residue | Details |
B | LYS73 |