3KGX
Crystal structure of Putative aminotransferase (AAH25799.1) from MUS MUSCULUS at 1.80 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004760 | molecular_function | L-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 | 0016740 | molecular_function | transferase activity |
| A | 0019265 | biological_process | glycine biosynthetic process, by transamination of glyoxylate |
| A | 0019448 | biological_process | L-cysteine catabolic process |
| A | 0019752 | biological_process | carboxylic acid metabolic 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 | 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 | L-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 | 0016740 | molecular_function | transferase activity |
| B | 0019265 | biological_process | glycine biosynthetic process, by transamination of glyoxylate |
| B | 0019448 | biological_process | L-cysteine catabolic process |
| B | 0019752 | biological_process | carboxylic acid metabolic 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 | 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 | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 502 |
| Chain | Residue |
| A | ASN54 |
| A | LEU55 |
| A | HOH789 |
| B | MET67 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 503 |
| Chain | Residue |
| A | HIS319 |
| A | HIS323 |
| A | ASP396 |
| A | HOH678 |
| A | HOH679 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 504 |
| Chain | Residue |
| A | GLU315 |
| A | THR392 |
| A | HOH700 |
| A | HOH744 |
| B | ARG403 |
| B | HOH740 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 505 |
| Chain | Residue |
| A | PHE113 |
| A | LEU116 |
| A | GLU117 |
| A | PRO118 |
| A | ILE141 |
| A | ARG255 |
| A | PRO259 |
| A | VAL260 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 507 |
| Chain | Residue |
| A | ARG93 |
| A | PRO95 |
| A | VAL145 |
| A | ASP246 |
| A | HOH603 |
| A | HOH626 |
| A | HOH813 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 508 |
| Chain | Residue |
| A | PRO187 |
| A | LEU188 |
| A | ASP189 |
| A | HOH628 |
| A | HOH801 |
| A | HOH820 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 510 |
| Chain | Residue |
| A | GLU109 |
| B | GLU109 |
| B | HOH665 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 511 |
| Chain | Residue |
| A | GLY190 |
| A | HOH672 |
| A | HOH681 |
| B | ARG255 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 501 |
| Chain | Residue |
| A | ARG66 |
| A | MET67 |
| B | ASN54 |
| B | LEU55 |
| B | HOH768 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 506 |
| Chain | Residue |
| B | PHE113 |
| B | LEU116 |
| B | GLU117 |
| B | ILE141 |
| B | ARG255 |
| B | PRO259 |
| B | VAL260 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 509 |
| Chain | Residue |
| B | ILE129 |
| B | ARG133 |
| B | HOH671 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 512 |
| Chain | Residue |
| B | LEU188 |
| B | ASP189 |
| B | HOH620 |
| B | HOH758 |
| B | HOH814 |
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 site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23576753","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
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 |
