2CH2
Structure of the Anopheles gambiae 3-hydroxykynurenine transaminase in complex with inhibitor
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 | 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 | 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 | 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 | 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 | 11 |
Details | BINDING SITE FOR RESIDUE KY1 C 1390 |
Chain | Residue |
B | PRO24 |
C | TYR256 |
C | THR259 |
B | GLY25 |
B | SER154 |
B | LYS205 |
B | GLN344 |
B | ARG356 |
B | PLP1390 |
C | SER43 |
C | ASN44 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PLP C 1391 |
Chain | Residue |
B | TYR256 |
B | THR259 |
B | KY11391 |
C | SER77 |
C | ALA78 |
C | HIS79 |
C | TRP104 |
C | GLY152 |
C | SER154 |
C | ASP179 |
C | VAL181 |
C | ALA182 |
C | GLN204 |
C | LYS205 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE KY1 D 1390 |
Chain | Residue |
A | GLY25 |
A | SER154 |
A | LYS205 |
A | GLN344 |
A | LEU347 |
A | ARG356 |
A | PLP1390 |
A | HOH2006 |
D | SER43 |
D | ASN44 |
D | PHE45 |
D | TYR256 |
D | HOH2019 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PLP D 1391 |
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 | KY11392 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PLP A 1390 |
Chain | Residue |
A | SER77 |
A | ALA78 |
A | HIS79 |
A | TRP104 |
A | GLY152 |
A | SER154 |
A | ASP179 |
A | VAL181 |
A | ALA182 |
A | GLN204 |
A | LYS205 |
D | TYR256 |
D | THR259 |
D | KY11390 |
site_id | AC6 |
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 |
C | TYR256 |
C | THR259 |
C | KY11390 |
site_id | AC7 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE KY1 B 1391 |
Chain | Residue |
B | SER43 |
B | ASN44 |
B | PHE45 |
B | TYR256 |
B | THR259 |
C | GLY25 |
C | TRP104 |
C | LYS205 |
C | GLN344 |
C | LEU347 |
C | ARG356 |
C | PLP1391 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE KY1 D 1392 |
Chain | Residue |
D | GLN344 |
D | ARG356 |
D | PLP1391 |
A | SER43 |
A | ASN44 |
A | TYR256 |
D | PRO24 |
D | GLY25 |
D | TRP104 |
D | SER154 |
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 |