1TB3
Crystal Structure Analysis of Recombinant Rat Kidney Long-chain Hydroxy Acid Oxidase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001561 | biological_process | fatty acid alpha-oxidation |
A | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
A | 0005777 | cellular_component | peroxisome |
A | 0005782 | cellular_component | peroxisomal matrix |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0010181 | molecular_function | FMN binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0018924 | biological_process | mandelate metabolic process |
A | 0019395 | biological_process | fatty acid oxidation |
A | 0042802 | molecular_function | identical protein binding |
B | 0001561 | biological_process | fatty acid alpha-oxidation |
B | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
B | 0005777 | cellular_component | peroxisome |
B | 0005782 | cellular_component | peroxisomal matrix |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0010181 | molecular_function | FMN binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0018924 | biological_process | mandelate metabolic process |
B | 0019395 | biological_process | fatty acid oxidation |
B | 0042802 | molecular_function | identical protein binding |
C | 0001561 | biological_process | fatty acid alpha-oxidation |
C | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
C | 0005777 | cellular_component | peroxisome |
C | 0005782 | cellular_component | peroxisomal matrix |
C | 0006631 | biological_process | fatty acid metabolic process |
C | 0010181 | molecular_function | FMN binding |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0018924 | biological_process | mandelate metabolic process |
C | 0019395 | biological_process | fatty acid oxidation |
C | 0042802 | molecular_function | identical protein binding |
D | 0001561 | biological_process | fatty acid alpha-oxidation |
D | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
D | 0005777 | cellular_component | peroxisome |
D | 0005782 | cellular_component | peroxisomal matrix |
D | 0006631 | biological_process | fatty acid metabolic process |
D | 0010181 | molecular_function | FMN binding |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0018924 | biological_process | mandelate metabolic process |
D | 0019395 | biological_process | fatty acid oxidation |
D | 0042802 | molecular_function | identical protein binding |
E | 0001561 | biological_process | fatty acid alpha-oxidation |
E | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
E | 0005777 | cellular_component | peroxisome |
E | 0005782 | cellular_component | peroxisomal matrix |
E | 0006631 | biological_process | fatty acid metabolic process |
E | 0010181 | molecular_function | FMN binding |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0018924 | biological_process | mandelate metabolic process |
E | 0019395 | biological_process | fatty acid oxidation |
E | 0042802 | molecular_function | identical protein binding |
F | 0001561 | biological_process | fatty acid alpha-oxidation |
F | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
F | 0005777 | cellular_component | peroxisome |
F | 0005782 | cellular_component | peroxisomal matrix |
F | 0006631 | biological_process | fatty acid metabolic process |
F | 0010181 | molecular_function | FMN binding |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0018924 | biological_process | mandelate metabolic process |
F | 0019395 | biological_process | fatty acid oxidation |
F | 0042802 | molecular_function | identical protein binding |
G | 0001561 | biological_process | fatty acid alpha-oxidation |
G | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
G | 0005777 | cellular_component | peroxisome |
G | 0005782 | cellular_component | peroxisomal matrix |
G | 0006631 | biological_process | fatty acid metabolic process |
G | 0010181 | molecular_function | FMN binding |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0018924 | biological_process | mandelate metabolic process |
G | 0019395 | biological_process | fatty acid oxidation |
G | 0042802 | molecular_function | identical protein binding |
H | 0001561 | biological_process | fatty acid alpha-oxidation |
H | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
H | 0005777 | cellular_component | peroxisome |
H | 0005782 | cellular_component | peroxisomal matrix |
H | 0006631 | biological_process | fatty acid metabolic process |
H | 0010181 | molecular_function | FMN binding |
H | 0016491 | molecular_function | oxidoreductase activity |
H | 0018924 | biological_process | mandelate metabolic process |
H | 0019395 | biological_process | fatty acid oxidation |
H | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE FMN A 1401 |
Chain | Residue |
A | PHE23 |
A | LYS223 |
A | SER245 |
A | HIS247 |
A | ARG250 |
A | ASP278 |
A | GLY279 |
A | GLY280 |
A | ARG282 |
A | GLY301 |
A | ARG302 |
A | ILE24 |
A | LEU305 |
A | ACY1402 |
A | HOH1410 |
A | HOH1415 |
A | PRO76 |
A | THR77 |
A | ALA78 |
A | SER105 |
A | GLN127 |
A | TYR129 |
A | THR155 |
site_id | AC2 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE FMN B 2401 |
Chain | Residue |
B | PHE23 |
B | ILE24 |
B | PRO76 |
B | THR77 |
B | ALA78 |
B | SER105 |
B | GLN127 |
B | TYR129 |
B | THR155 |
B | LYS223 |
B | SER245 |
B | HIS247 |
B | ARG250 |
B | ASP278 |
B | GLY279 |
B | GLY280 |
B | ARG282 |
B | GLY301 |
B | ARG302 |
B | LEU305 |
B | ACY2402 |
B | HOH2411 |
B | HOH2423 |
site_id | AC3 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE FMN C 3401 |
Chain | Residue |
C | PHE23 |
C | ILE24 |
C | PRO76 |
C | THR77 |
C | ALA78 |
C | SER105 |
C | GLN127 |
C | TYR129 |
C | THR155 |
C | LYS223 |
C | SER245 |
C | HIS247 |
C | ARG250 |
C | ASP278 |
C | GLY279 |
C | GLY280 |
C | ARG282 |
C | GLY301 |
C | ARG302 |
C | LEU305 |
C | ACY3402 |
C | HOH3405 |
C | HOH3445 |
site_id | AC4 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE FMN D 4401 |
Chain | Residue |
D | PHE23 |
D | ILE24 |
D | PRO76 |
D | THR77 |
D | ALA78 |
D | SER105 |
D | GLN127 |
D | TYR129 |
D | THR155 |
D | LYS223 |
D | SER245 |
D | HIS247 |
D | ARG250 |
D | ASP278 |
D | GLY279 |
D | GLY280 |
D | ARG282 |
D | GLY301 |
D | ARG302 |
D | LEU305 |
D | ACY4402 |
D | HOH4421 |
D | HOH4422 |
site_id | AC5 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE FMN E 5401 |
Chain | Residue |
E | GLN127 |
E | TYR129 |
E | THR155 |
E | LYS223 |
E | SER245 |
E | HIS247 |
E | GLY248 |
E | ARG250 |
E | ASP278 |
E | GLY279 |
E | GLY280 |
E | ARG282 |
E | GLY301 |
E | ARG302 |
E | LEU305 |
E | ACY5402 |
E | HOH5425 |
E | HOH5426 |
E | PHE23 |
E | ILE24 |
E | SER75 |
E | PRO76 |
E | THR77 |
E | ALA78 |
E | SER105 |
site_id | AC6 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE FMN F 6401 |
Chain | Residue |
F | PHE23 |
F | ILE24 |
F | PRO76 |
F | THR77 |
F | ALA78 |
F | SER105 |
F | GLN127 |
F | TYR129 |
F | THR155 |
F | LYS223 |
F | SER245 |
F | HIS247 |
F | ARG250 |
F | ASP278 |
F | GLY279 |
F | GLY280 |
F | ARG282 |
F | GLY301 |
F | ARG302 |
F | LEU305 |
F | ACY6402 |
F | HOH6408 |
F | HOH6421 |
site_id | AC7 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE FMN G 7401 |
Chain | Residue |
G | PHE23 |
G | ILE24 |
G | PRO76 |
G | THR77 |
G | ALA78 |
G | SER105 |
G | GLN127 |
G | TYR129 |
G | THR155 |
G | LYS223 |
G | SER245 |
G | HIS247 |
G | ARG250 |
G | ASP278 |
G | GLY279 |
G | GLY280 |
G | ARG282 |
G | GLY301 |
G | ARG302 |
G | LEU305 |
G | ACY7402 |
G | HOH7409 |
G | HOH7427 |
site_id | AC8 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE FMN H 8401 |
Chain | Residue |
H | PHE23 |
H | ILE24 |
H | PRO76 |
H | THR77 |
H | ALA78 |
H | SER105 |
H | GLN127 |
H | TYR129 |
H | THR155 |
H | LYS223 |
H | SER245 |
H | HIS247 |
H | ARG250 |
H | ASP278 |
H | GLY279 |
H | GLY280 |
H | ARG282 |
H | GLY301 |
H | ARG302 |
H | LEU305 |
H | ACY8402 |
H | HOH8403 |
H | HOH8441 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACY A 1402 |
Chain | Residue |
A | TYR129 |
A | ARG164 |
A | HIS247 |
A | ARG250 |
A | FMN1401 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACY B 2402 |
Chain | Residue |
B | TYR129 |
B | ARG164 |
B | HIS247 |
B | ARG250 |
B | FMN2401 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACY C 3402 |
Chain | Residue |
C | TYR129 |
C | ARG164 |
C | HIS247 |
C | FMN3401 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACY D 4402 |
Chain | Residue |
D | TYR129 |
D | ARG164 |
D | HIS247 |
D | FMN4401 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACY E 5402 |
Chain | Residue |
E | TYR129 |
E | ARG164 |
E | HIS247 |
E | ARG250 |
E | FMN5401 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACY F 6402 |
Chain | Residue |
F | TYR129 |
F | ARG164 |
F | HIS247 |
F | ARG250 |
F | FMN6401 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACY G 7402 |
Chain | Residue |
G | TYR129 |
G | ARG164 |
G | HIS247 |
G | FMN7401 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACY H 8402 |
Chain | Residue |
H | TYR129 |
H | ARG164 |
H | HIS247 |
H | FMN8401 |
Functional Information from PROSITE/UniProt
site_id | PS00557 |
Number of Residues | 7 |
Details | FMN_HYDROXY_ACID_DH_1 FMN-dependent alpha-hydroxy acid dehydrogenases active site. SNHGGRQ |
Chain | Residue | Details |
A | SER245-GLN251 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00683, ECO:0000305|PubMed:15683236 |
Chain | Residue | Details |
A | GLY248 | |
B | GLY248 | |
C | GLY248 | |
D | GLY248 | |
E | GLY248 | |
F | GLY248 | |
G | GLY248 | |
H | GLY248 |
site_id | SWS_FT_FI2 |
Number of Residues | 56 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15683236, ECO:0000269|PubMed:22342614, ECO:0007744|PDB:1TB3, ECO:0007744|PDB:3SGZ |
Chain | Residue | Details |
A | THR77 | |
B | LEU128 | |
B | ILE156 | |
B | GLY224 | |
B | GLY279 | |
B | ARG302 | |
C | THR77 | |
C | SER106 | |
C | LEU128 | |
C | ILE156 | |
C | GLY224 | |
A | SER106 | |
C | GLY279 | |
C | ARG302 | |
D | THR77 | |
D | SER106 | |
D | LEU128 | |
D | ILE156 | |
D | GLY224 | |
D | GLY279 | |
D | ARG302 | |
E | THR77 | |
A | LEU128 | |
E | SER106 | |
E | LEU128 | |
E | ILE156 | |
E | GLY224 | |
E | GLY279 | |
E | ARG302 | |
F | THR77 | |
F | SER106 | |
F | LEU128 | |
F | ILE156 | |
A | ILE156 | |
F | GLY224 | |
F | GLY279 | |
F | ARG302 | |
G | THR77 | |
G | SER106 | |
G | LEU128 | |
G | ILE156 | |
G | GLY224 | |
G | GLY279 | |
G | ARG302 | |
A | GLY224 | |
H | THR77 | |
H | SER106 | |
H | LEU128 | |
H | ILE156 | |
H | GLY224 | |
H | GLY279 | |
H | ARG302 | |
A | GLY279 | |
A | ARG302 | |
B | THR77 | |
B | SER106 |
site_id | SWS_FT_FI3 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00683 |
Chain | Residue | Details |
A | MET130 | |
D | MET130 | |
D | ARG165 | |
D | GLN251 | |
E | MET130 | |
E | ARG165 | |
E | GLN251 | |
F | MET130 | |
F | ARG165 | |
F | GLN251 | |
G | MET130 | |
A | ARG165 | |
G | ARG165 | |
G | GLN251 | |
H | MET130 | |
H | ARG165 | |
H | GLN251 | |
A | GLN251 | |
B | MET130 | |
B | ARG165 | |
B | GLN251 | |
C | MET130 | |
C | ARG165 | |
C | GLN251 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
Chain | Residue | Details |
A | ASP133 | |
B | ASP133 | |
C | ASP133 | |
D | ASP133 | |
E | ASP133 | |
F | ASP133 | |
G | ASP133 | |
H | ASP133 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1gox |
Chain | Residue | Details |
A | TYR129 | |
A | HIS247 | |
A | ASP157 | |
A | ARG250 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1gox |
Chain | Residue | Details |
B | TYR129 | |
B | HIS247 | |
B | ASP157 | |
B | ARG250 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1gox |
Chain | Residue | Details |
C | TYR129 | |
C | HIS247 | |
C | ASP157 | |
C | ARG250 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1gox |
Chain | Residue | Details |
D | TYR129 | |
D | HIS247 | |
D | ASP157 | |
D | ARG250 |
site_id | CSA5 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1gox |
Chain | Residue | Details |
E | TYR129 | |
E | HIS247 | |
E | ASP157 | |
E | ARG250 |
site_id | CSA6 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1gox |
Chain | Residue | Details |
F | TYR129 | |
F | HIS247 | |
F | ASP157 | |
F | ARG250 |
site_id | CSA7 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1gox |
Chain | Residue | Details |
G | TYR129 | |
G | HIS247 | |
G | ASP157 | |
G | ARG250 |
site_id | CSA8 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1gox |
Chain | Residue | Details |
H | TYR129 | |
H | HIS247 | |
H | ASP157 | |
H | ARG250 |