3CSW
Crystal structure of a putative branched-chain amino acid aminotransferase (TM0831) from Thermotoga maritima at 2.15 A resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0008483 | molecular_function | transaminase activity |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
A | 0009097 | biological_process | isoleucine biosynthetic process |
A | 0009098 | biological_process | L-leucine biosynthetic process |
A | 0009099 | biological_process | valine biosynthetic process |
A | 0019752 | biological_process | carboxylic acid metabolic process |
A | 0046394 | biological_process | carboxylic acid biosynthetic process |
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 |
B | 0003824 | molecular_function | catalytic activity |
B | 0008483 | molecular_function | transaminase activity |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
B | 0009097 | biological_process | isoleucine biosynthetic process |
B | 0009098 | biological_process | L-leucine biosynthetic process |
B | 0009099 | biological_process | valine biosynthetic process |
B | 0019752 | biological_process | carboxylic acid metabolic process |
B | 0046394 | biological_process | carboxylic acid biosynthetic process |
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 |
C | 0003824 | molecular_function | catalytic activity |
C | 0008483 | molecular_function | transaminase activity |
C | 0008652 | biological_process | amino acid biosynthetic process |
C | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
C | 0009097 | biological_process | isoleucine biosynthetic process |
C | 0009098 | biological_process | L-leucine biosynthetic process |
C | 0009099 | biological_process | valine biosynthetic process |
C | 0019752 | biological_process | carboxylic acid metabolic process |
C | 0046394 | biological_process | carboxylic acid biosynthetic process |
C | 0050048 | molecular_function | L-leucine:2-oxoglutarate aminotransferase activity |
C | 0052654 | molecular_function | L-leucine transaminase activity |
C | 0052655 | molecular_function | L-valine transaminase activity |
C | 0052656 | molecular_function | L-isoleucine transaminase activity |
D | 0003824 | molecular_function | catalytic activity |
D | 0008483 | molecular_function | transaminase activity |
D | 0008652 | biological_process | amino acid biosynthetic process |
D | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
D | 0009097 | biological_process | isoleucine biosynthetic process |
D | 0009098 | biological_process | L-leucine biosynthetic process |
D | 0009099 | biological_process | valine biosynthetic process |
D | 0019752 | biological_process | carboxylic acid metabolic process |
D | 0046394 | biological_process | carboxylic acid biosynthetic process |
D | 0050048 | molecular_function | L-leucine:2-oxoglutarate aminotransferase activity |
D | 0052654 | molecular_function | L-leucine transaminase activity |
D | 0052655 | molecular_function | L-valine transaminase activity |
D | 0052656 | molecular_function | L-isoleucine transaminase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE PLP A 300 |
Chain | Residue |
A | ARG50 |
A | ASN169 |
A | LEU188 |
A | GLY190 |
A | ILE191 |
A | THR192 |
A | THR228 |
A | LYS133 |
A | ILE140 |
A | ARG144 |
A | GLU164 |
A | GLY165 |
A | SER166 |
A | PHE167 |
A | SER168 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PLP C 300 |
Chain | Residue |
C | ARG50 |
C | LYS133 |
C | GLU164 |
C | SER166 |
C | PHE167 |
C | SER168 |
C | ASN169 |
C | LEU188 |
C | GLY190 |
C | ILE191 |
C | THR192 |
C | THR228 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE UNL B 276 |
Chain | Residue |
B | ARG85 |
B | HIS227 |
B | THR228 |
B | SER229 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE UNL C 301 |
Chain | Residue |
C | THR33 |
C | HIS227 |
C | THR228 |
C | SER229 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE UNL A 301 |
Chain | Residue |
A | THR33 |
A | HIS227 |
A | THR228 |
A | SER229 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE UNL D 275 |
Chain | Residue |
D | THR33 |
D | ARG85 |
D | HIS227 |
D | THR228 |
D | SER229 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CIT A 302 |
Chain | Residue |
A | LEU142 |
A | ARG145 |
A | GLU146 |
B | PHE57 |
B | PHE58 |
C | ASP67 |
C | LYS71 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CIT D 276 |
Chain | Residue |
D | ARG122 |
D | PRO124 |
D | ASP125 |
D | LEU126 |
D | ASN159 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CIT B 277 |
Chain | Residue |
B | ARG122 |
B | PRO124 |
B | ASP125 |
B | LEU126 |
B | LEU158 |
B | ASN159 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MPD A 303 |
Chain | Residue |
A | ASN159 |
A | ASP184 |
A | SER185 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MPD A 304 |
Chain | Residue |
A | ASP125 |
A | PRO129 |
B | ASN119 |
site_id | BC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MPD C 303 |
Chain | Residue |
C | ASP184 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MPD B 278 |
Chain | Residue |
B | LYS52 |
B | ASP56 |
B | ASN59 |
B | LEU60 |
C | PHE66 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MPD B 279 |
Chain | Residue |
B | ASP125 |
B | LEU126 |
B | SER127 |
B | THR128 |
B | PRO129 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MPD D 277 |
Chain | Residue |
C | ASN119 |
D | PHE57 |
D | LEU126 |
D | SER127 |
D | THR128 |
D | PRO129 |
Functional Information from PROSITE/UniProt
site_id | PS00770 |
Number of Residues | 30 |
Details | AA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EgSfsNVFlvkegk......LiTpsldsgi.LdGItR |
Chain | Residue | Details |
A | GLU164-ARG193 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
Chain | Residue | Details |
A | LYS133 | |
B | LYS133 | |
C | LYS133 | |
D | LYS133 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1daa |
Chain | Residue | Details |
A | LYS133 | |
A | GLU164 | |
A | LEU188 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1daa |
Chain | Residue | Details |
B | LYS133 | |
B | GLU164 | |
B | LEU188 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1daa |
Chain | Residue | Details |
C | LYS133 | |
C | GLU164 | |
C | LEU188 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1daa |
Chain | Residue | Details |
D | LYS133 | |
D | GLU164 | |
D | LEU188 |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1daa |
Chain | Residue | Details |
A | LYS133 |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1daa |
Chain | Residue | Details |
B | LYS133 |
site_id | CSA7 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1daa |
Chain | Residue | Details |
C | LYS133 |
site_id | CSA8 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1daa |
Chain | Residue | Details |
D | LYS133 |