5CR5
X-RAY CRYSTAL STRUCTURE AT 1.61A RESOLUTION OF HUMAN MITOCHONDRIAL BRANCHED CHAIN AMINOTRANSFERASE (BCATM) COMPLEXED WITH A BIPHENYL PYRROLIDINE ETHER COMPOUND AND AN INTERNAL ALDIMINE LINKED PLP COFACTOR.
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 | 16 |
| Details | binding site for residue PLP A 401 |
| Chain | Residue |
| A | ARG99 |
| A | VAL270 |
| A | GLY312 |
| A | THR313 |
| A | EL1402 |
| A | HOH548 |
| A | HOH662 |
| A | HOH718 |
| A | LYS202 |
| A | TYR207 |
| A | GLU237 |
| A | THR240 |
| A | ASN242 |
| A | LEU266 |
| A | GLY268 |
| A | VAL269 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | binding site for residue EL1 A 402 |
| Chain | Residue |
| A | PHE30 |
| A | PHE75 |
| A | ARG143 |
| A | TYR173 |
| A | VAL182 |
| A | GLN224 |
| A | VAL238 |
| A | GLY239 |
| A | THR240 |
| A | MET241 |
| A | GLY312 |
| A | THR313 |
| A | ALA314 |
| A | CYS318 |
| A | PLP401 |
| A | HOH522 |
| A | HOH612 |
| B | TYR70 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 403 |
| Chain | Residue |
| A | LYS79 |
| A | GLN316 |
| A | HOH654 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | TYR246 |
| A | ARG306 |
| A | ARG344 |
| A | HOH519 |
| A | HOH568 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | GLN234 |
| A | ASN262 |
| A | THR290 |
| A | HOH524 |
| A | HOH566 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | ILE191 |
| A | TRP194 |
| A | TYR229 |
| A | GLY230 |
| A | HOH529 |
| A | HOH601 |
| A | HOH637 |
| B | TRP194 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | GLU42 |
| A | LEU59 |
| A | THR60 |
| A | HOH647 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 408 |
| Chain | Residue |
| A | LEU261 |
| A | ASN262 |
| A | HOH809 |
| B | ALA358 |
| B | HIS359 |
| site_id | AC9 |
| Number of Residues | 17 |
| Details | binding site for residue EL1 B 402 |
| Chain | Residue |
| A | TYR70 |
| B | PHE30 |
| B | ARG143 |
| B | TYR173 |
| B | VAL182 |
| B | GLN224 |
| B | VAL238 |
| B | GLY239 |
| B | THR240 |
| B | MET241 |
| B | GLY312 |
| B | THR313 |
| B | ALA314 |
| B | CYS318 |
| B | PLP401 |
| B | HOH514 |
| B | HOH529 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 403 |
| Chain | Residue |
| B | LYS79 |
| B | GLN316 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 404 |
| Chain | Residue |
| B | TYR246 |
| B | ARG306 |
| B | GLU340 |
| B | ARG344 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 405 |
| Chain | Residue |
| B | GLU42 |
| B | LEU59 |
| B | THR60 |
| B | HOH684 |
| site_id | AD4 |
| Number of Residues | 21 |
| Details | binding site for Di-peptide PLP B 401 and LYS B 202 |
| Chain | Residue |
| B | THR240 |
| B | ASN242 |
| B | LEU266 |
| B | GLY268 |
| B | VAL269 |
| B | VAL270 |
| B | GLY312 |
| B | THR313 |
| B | EL1402 |
| B | HOH502 |
| B | HOH519 |
| B | HOH599 |
| B | HOH721 |
| B | LEU74 |
| B | PHE75 |
| B | ARG99 |
| B | SER103 |
| B | TYR201 |
| B | LEU203 |
| B | TYR207 |
| B | GLU237 |
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 |
