1KTA
HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE : THREE DIMENSIONAL STRUCTURE OF THE ENZYME IN ITS PYRIDOXAMINE PHOSPHATE FORM.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004084 | molecular_function | branched-chain-amino-acid transaminase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009081 | biological_process | branched-chain amino acid metabolic process |
| A | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| A | 0009083 | biological_process | branched-chain amino acid catabolic process |
| A | 0009098 | biological_process | L-leucine biosynthetic process |
| A | 0009099 | biological_process | L-valine biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0050873 | biological_process | brown fat cell differentiation |
| A | 0052654 | molecular_function | L-leucine-2-oxoglutarate transaminase activity |
| A | 0052655 | molecular_function | L-valine-2-oxoglutarate transaminase activity |
| A | 0052656 | molecular_function | L-isoleucine-2-oxoglutarate transaminase activity |
| A | 0097009 | biological_process | energy homeostasis |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004084 | molecular_function | branched-chain-amino-acid transaminase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009081 | biological_process | branched-chain amino acid metabolic process |
| B | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| B | 0009083 | biological_process | branched-chain amino acid catabolic process |
| B | 0009098 | biological_process | L-leucine biosynthetic process |
| B | 0009099 | biological_process | L-valine biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0050873 | biological_process | brown fat cell differentiation |
| B | 0052654 | molecular_function | L-leucine-2-oxoglutarate transaminase activity |
| B | 0052655 | molecular_function | L-valine-2-oxoglutarate transaminase activity |
| B | 0052656 | molecular_function | L-isoleucine-2-oxoglutarate transaminase activity |
| B | 0097009 | biological_process | energy homeostasis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE KIV B 3001 |
| Chain | Residue |
| A | PHE75 |
| A | LYS202 |
| A | TYR207 |
| A | PMP400 |
| A | HOH1014 |
| B | TYR570 |
| B | VAL655 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PMP A 400 |
| Chain | Residue |
| A | LYS202 |
| A | TYR207 |
| A | GLU237 |
| A | THR240 |
| A | ASN242 |
| A | LEU266 |
| A | GLY268 |
| A | VAL269 |
| A | VAL270 |
| A | GLY312 |
| A | THR313 |
| A | HOH1008 |
| A | HOH1079 |
| A | HOH1122 |
| B | KIV3001 |
| A | ARG99 |
| A | ARG192 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PMP B 900 |
| Chain | Residue |
| B | HOH2 |
| B | HOH14 |
| B | HOH89 |
| B | ARG599 |
| B | ARG692 |
| B | LYS702 |
| B | TYR707 |
| B | GLU737 |
| B | THR740 |
| B | MET741 |
| B | ASN742 |
| B | LEU766 |
| B | GLY768 |
| B | VAL769 |
| B | VAL770 |
| B | GLY812 |
| B | THR813 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACY B 1001 |
| Chain | Residue |
| B | HOH124 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACY B 1002 |
| Chain | Residue |
| B | HOH242 |
| B | GLU840 |
| B | LEU843 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY A 1003 |
| Chain | Residue |
| A | ARG102 |
| A | ASN200 |
| A | LEU261 |
| A | PRO267 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACY B 1004 |
| Chain | Residue |
| B | LYS847 |
| B | GLU851 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACY B 1005 |
| Chain | Residue |
| B | HOH98 |
| B | GLY696 |
| B | GLY697 |
| B | ASN700 |
| B | TYR701 |
| B | GLY763 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACY A 1006 |
| Chain | Residue |
| A | ARG92 |
| A | TRP94 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACY A 1007 |
| Chain | Residue |
| A | ARG102 |
| A | MET105 |
| A | HOH1061 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 2001 |
| Chain | Residue |
| B | ASP776 |
| B | MET777 |
| B | THR780 |
| B | HIS859 |
| B | TRP861 |
Functional Information from PROSITE/UniProt
| site_id | PS00770 |
| Number of Residues | 35 |
| Details | AA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EvGtmNIFvywthedgvle.LvTpplngvi.LpGVvR |
| Chain | Residue | Details |
| A | GLU237-ARG271 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12269802","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16141215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17050531","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"16141215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17050531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2A1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HDK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HG8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HGW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HGX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HHF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1iyd |
| Chain | Residue | Details |
| A | LYS202 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1iyd |
| Chain | Residue | Details |
| B | LYS702 |
