1KT8
HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL): THREE DIMENSIONAL STRUCTURE OF ENZYME IN ITS KETIMINE FORM WITH THE SUBSTRATE L-ISOLEUCINE
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 | 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 | L-valine biosynthetic process |
| A | 0010817 | biological_process | regulation of hormone levels |
| 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 | 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 | 0005515 | molecular_function | protein binding |
| 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 | L-valine biosynthetic process |
| B | 0010817 | biological_process | regulation of hormone levels |
| 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 | 1990830 | biological_process | cellular response to leukemia inhibitory factor |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ILP A 400 |
| Chain | Residue |
| A | GLY77 |
| A | LEU266 |
| A | GLY268 |
| A | VAL269 |
| A | VAL270 |
| A | GLY312 |
| A | THR313 |
| A | HOH1032 |
| A | HOH1036 |
| A | ARG99 |
| A | TYR141 |
| A | ARG192 |
| A | LYS202 |
| A | TYR207 |
| A | GLU237 |
| A | THR240 |
| A | ASN242 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ILP B 900 |
| Chain | Residue |
| A | TYR70 |
| A | VAL155 |
| B | HOH68 |
| B | HOH108 |
| B | HOH119 |
| B | PHE575 |
| B | GLY577 |
| B | ARG599 |
| B | TYR641 |
| B | ARG643 |
| B | ARG692 |
| B | LYS702 |
| B | TYR707 |
| B | GLU737 |
| B | THR740 |
| B | ASN742 |
| B | LEU766 |
| B | GLY768 |
| B | VAL769 |
| B | VAL770 |
| B | THR813 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY B 1001 |
| Chain | Residue |
| B | MET540 |
| B | GLU542 |
| B | THR560 |
| B | LEU662 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY B 1002 |
| Chain | Residue |
| B | ASP776 |
| B | MET777 |
| B | THR780 |
| B | HIS859 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY A 1003 |
| Chain | Residue |
| A | ARG102 |
| A | ASN200 |
| A | LEU261 |
| A | PRO267 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACY A 1004 |
| Chain | Residue |
| A | TRP94 |
| A | ACY1005 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACY A 1005 |
| Chain | Residue |
| A | ARG92 |
| A | TRP94 |
| A | ACY1004 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACY B 1006 |
| Chain | Residue |
| B | ARG592 |
| B | TRP594 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 2001 |
| Chain | Residue |
| B | HOH181 |
| B | PHE690 |
| B | LEU712 |
| B | VAL713 |
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 |
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 |
