2CH1
Structure of Anopheles gambiae 3-hydroxykynurenine transaminase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004760 | molecular_function | serine-pyruvate transaminase activity |
| A | 0005777 | cellular_component | peroxisome |
| A | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009436 | biological_process | glyoxylate catabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019265 | biological_process | glycine biosynthetic process, by transamination of glyoxylate |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0036137 | molecular_function | kynurenine aminotransferase activity |
| A | 0047315 | molecular_function | kynurenine-glyoxylate transaminase activity |
| A | 0097053 | biological_process | L-kynurenine catabolic process |
| B | 0004760 | molecular_function | serine-pyruvate transaminase activity |
| B | 0005777 | cellular_component | peroxisome |
| B | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009436 | biological_process | glyoxylate catabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019265 | biological_process | glycine biosynthetic process, by transamination of glyoxylate |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0036137 | molecular_function | kynurenine aminotransferase activity |
| B | 0047315 | molecular_function | kynurenine-glyoxylate transaminase activity |
| B | 0097053 | biological_process | L-kynurenine catabolic process |
| C | 0004760 | molecular_function | serine-pyruvate transaminase activity |
| C | 0005777 | cellular_component | peroxisome |
| C | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009436 | biological_process | glyoxylate catabolic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0019265 | biological_process | glycine biosynthetic process, by transamination of glyoxylate |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0036137 | molecular_function | kynurenine aminotransferase activity |
| C | 0047315 | molecular_function | kynurenine-glyoxylate transaminase activity |
| C | 0097053 | biological_process | L-kynurenine catabolic process |
| D | 0004760 | molecular_function | serine-pyruvate transaminase activity |
| D | 0005777 | cellular_component | peroxisome |
| D | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009436 | biological_process | glyoxylate catabolic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0019265 | biological_process | glycine biosynthetic process, by transamination of glyoxylate |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0036137 | molecular_function | kynurenine aminotransferase activity |
| D | 0047315 | molecular_function | kynurenine-glyoxylate transaminase activity |
| D | 0097053 | biological_process | L-kynurenine catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP A 1390 |
| Chain | Residue |
| A | SER77 |
| A | GLN204 |
| A | LYS205 |
| A | GOL1391 |
| D | TYR256 |
| D | THR259 |
| A | ALA78 |
| A | HIS79 |
| A | TRP104 |
| A | GLY152 |
| A | SER154 |
| A | ASP179 |
| A | VAL181 |
| A | ALA182 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP B 1390 |
| Chain | Residue |
| B | SER77 |
| B | ALA78 |
| B | HIS79 |
| B | TRP104 |
| B | GLY152 |
| B | SER154 |
| B | ASP179 |
| B | VAL181 |
| B | ALA182 |
| B | GLN204 |
| B | LYS205 |
| B | GOL1391 |
| C | TYR256 |
| C | THR259 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP C 1390 |
| Chain | Residue |
| B | TYR256 |
| B | THR259 |
| C | SER77 |
| C | ALA78 |
| C | HIS79 |
| C | TRP104 |
| C | GLY152 |
| C | SER154 |
| C | ASP179 |
| C | VAL181 |
| C | ALA182 |
| C | GLN204 |
| C | LYS205 |
| C | GOL1391 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP D 1390 |
| Chain | Residue |
| A | TYR256 |
| A | THR259 |
| D | SER77 |
| D | ALA78 |
| D | HIS79 |
| D | TRP104 |
| D | GLY152 |
| D | SER154 |
| D | ASP179 |
| D | VAL181 |
| D | ALA182 |
| D | GLN204 |
| D | LYS205 |
| D | GOL1391 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1391 |
| Chain | Residue |
| A | TRP104 |
| A | SER154 |
| A | LYS205 |
| A | ARG356 |
| A | PLP1390 |
| A | HOH2011 |
| A | HOH2111 |
| D | THR259 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 1391 |
| Chain | Residue |
| B | TRP104 |
| B | SER154 |
| B | ARG356 |
| B | PLP1390 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 1391 |
| Chain | Residue |
| B | THR259 |
| C | TRP104 |
| C | LYS205 |
| C | ARG356 |
| C | PLP1390 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 1391 |
| Chain | Residue |
| A | THR259 |
| D | TRP104 |
| D | LYS205 |
| D | ARG356 |
| D | PLP1390 |
Functional Information from PROSITE/UniProt
| site_id | PS00595 |
| Number of Residues | 21 |
| Details | AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. IDAVytGAQKvlgappGiTpI |
| Chain | Residue | Details |
| A | ILE196-ILE216 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:16585514, ECO:0007744|PDB:2CH1, ECO:0007744|PDB:2CH2 |
| Chain | Residue | Details |
| A | SER77 | |
| A | GLN204 | |
| B | SER77 | |
| B | GLN204 | |
| C | SER77 | |
| C | GLN204 | |
| D | SER77 | |
| D | GLN204 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:16585514, ECO:0007744|PDB:2CH2 |
| Chain | Residue | Details |
| A | SER154 | |
| A | ARG356 | |
| B | SER154 | |
| B | ARG356 | |
| C | SER154 | |
| C | ARG356 | |
| D | SER154 | |
| D | ARG356 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16585514, ECO:0007744|PDB:2CH1, ECO:0007744|PDB:2CH2 |
| Chain | Residue | Details |
| A | TYR256 | |
| A | THR259 | |
| B | TYR256 | |
| B | THR259 | |
| C | TYR256 | |
| C | THR259 | |
| D | TYR256 | |
| D | THR259 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:16585514, ECO:0007744|PDB:2CH1, ECO:0007744|PDB:2CH2 |
| Chain | Residue | Details |
| A | LYS205 | |
| B | LYS205 | |
| C | LYS205 | |
| D | LYS205 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b9h |
| Chain | Residue | Details |
| A | ARG51 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b9h |
| Chain | Residue | Details |
| B | ARG51 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b9h |
| Chain | Residue | Details |
| C | ARG51 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b9h |
| Chain | Residue | Details |
| D | ARG51 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b9h |
| Chain | Residue | Details |
| A | ASP179 | |
| A | TRP104 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b9h |
| Chain | Residue | Details |
| B | ASP179 | |
| B | TRP104 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b9h |
| Chain | Residue | Details |
| C | ASP179 | |
| C | TRP104 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b9h |
| Chain | Residue | Details |
| D | ASP179 | |
| D | TRP104 |
