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 | 0005654 | cellular_component | nucleoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0006549 | biological_process | isoleucine metabolic process |
A | 0006550 | biological_process | isoleucine catabolic process |
A | 0006551 | biological_process | L-leucine metabolic process |
A | 0006573 | biological_process | valine metabolic process |
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 | valine biosynthetic process |
A | 0010817 | biological_process | regulation of hormone levels |
A | 0050048 | molecular_function | L-leucine:2-oxoglutarate aminotransferase activity |
A | 0052654 | molecular_function | L-leucine transaminase activity |
A | 0052655 | molecular_function | L-valine transaminase activity |
A | 0052656 | molecular_function | L-isoleucine transaminase activity |
A | 1990830 | biological_process | cellular response to leukemia inhibitory factor |
B | 0003824 | molecular_function | catalytic activity |
B | 0004084 | molecular_function | branched-chain-amino-acid transaminase activity |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0006549 | biological_process | isoleucine metabolic process |
B | 0006550 | biological_process | isoleucine catabolic process |
B | 0006551 | biological_process | L-leucine metabolic process |
B | 0006573 | biological_process | valine metabolic process |
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 | valine biosynthetic process |
B | 0010817 | biological_process | regulation of hormone levels |
B | 0050048 | molecular_function | L-leucine:2-oxoglutarate aminotransferase activity |
B | 0052654 | molecular_function | L-leucine transaminase activity |
B | 0052655 | molecular_function | L-valine transaminase activity |
B | 0052656 | molecular_function | L-isoleucine transaminase activity |
B | 1990830 | biological_process | cellular response to leukemia inhibitory factor |
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: BINDING => ECO:0000269|PubMed:12269802, ECO:0000269|PubMed:16141215, ECO:0000269|PubMed:17050531 |
Chain | Residue | Details |
A | TYR141 | |
B | TYR641 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:16141215, ECO:0000269|PubMed:17050531, ECO:0007744|PDB:2A1H, ECO:0007744|PDB:2HDK, ECO:0007744|PDB:2HG8, ECO:0007744|PDB:2HGW, ECO:0007744|PDB:2HGX, ECO:0007744|PDB:2HHF |
Chain | Residue | Details |
A | LYS202 | |
B | LYS702 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS294 | |
B | LYS794 |