2HGW
Crystal structure of Cys318Ala mutant of human mitochondrial branched chain aminotransferase
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 | L-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 | 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 | 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 | L-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 | 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 | 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 SO4 B 1012 |
| Chain | Residue |
| B | HOH147 |
| B | PLP401 |
| B | THR740 |
| B | MET741 |
| B | GLY812 |
| B | THR813 |
| B | ALA814 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP A 400 |
| Chain | Residue |
| A | LYS202 |
| A | TYR207 |
| A | GLU237 |
| A | THR240 |
| A | ASN242 |
| A | GLY268 |
| A | VAL269 |
| A | VAL270 |
| A | GLY312 |
| A | THR313 |
| A | ACY1003 |
| A | HOH2002 |
| A | HOH2011 |
| A | HOH2025 |
| A | ARG99 |
| A | ARG192 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP B 401 |
| Chain | Residue |
| B | HOH25 |
| B | HOH32 |
| B | HOH136 |
| B | ARG599 |
| B | ARG692 |
| B | LYS702 |
| B | TYR707 |
| B | GLU737 |
| B | THR740 |
| B | ASN742 |
| B | LEU766 |
| B | GLY768 |
| B | VAL769 |
| B | VAL770 |
| B | GLY812 |
| B | THR813 |
| B | SO41012 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EPE A 1011 |
| Chain | Residue |
| A | GLN50 |
| A | ASP327 |
| A | ARG328 |
| A | ASN329 |
| A | GOL2001 |
| A | HOH2044 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACY A 1001 |
| Chain | Residue |
| A | HIS62 |
| A | ASN149 |
| A | ARG160 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACY A 1002 |
| Chain | Residue |
| A | THR290 |
| A | GLN295 |
| B | ASP585 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACY A 1003 |
| Chain | Residue |
| A | THR240 |
| A | GLY312 |
| A | THR313 |
| A | ALA314 |
| A | PLP400 |
| A | HOH2057 |
| B | ACY1005 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACY A 1004 |
| Chain | Residue |
| A | THR15 |
| A | LYS17 |
| A | HIS19 |
| A | ASP36 |
| A | PHE56 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY B 1005 |
| Chain | Residue |
| A | PHE30 |
| A | ACY1003 |
| B | TYR570 |
| B | LEU653 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACY A 1006 |
| Chain | Residue |
| A | MET40 |
| A | GLU42 |
| A | THR60 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACY A 1007 |
| Chain | Residue |
| A | THR210 |
| A | GLN224 |
| A | THR240 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY A 1008 |
| Chain | Residue |
| A | LEU95 |
| A | ARG99 |
| A | ARG102 |
| A | PRO267 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACY A 1009 |
| Chain | Residue |
| A | ARG220 |
| A | ARG322 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACY B 1010 |
| Chain | Residue |
| B | ARG599 |
| B | ARG602 |
| B | PRO767 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 2001 |
| Chain | Residue |
| A | GLU42 |
| A | ASN44 |
| A | GLY47 |
| A | GLY49 |
| A | ASP327 |
| A | EPE1011 |
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 |
