Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0020037 | molecular_function | heme binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0020037 | molecular_function | heme binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO3 A 580 |
Chain | Residue |
A | TYR143 |
A | ALA198 |
A | TYR254 |
A | HIS373 |
A | ARG376 |
A | FMN570 |
A | HOH651 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO3 B 580 |
Chain | Residue |
B | TYR254 |
B | HIS373 |
B | ARG376 |
B | FMN570 |
B | TYR143 |
B | ALA198 |
site_id | AC3 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE FMN A 570 |
Chain | Residue |
A | TYR144 |
A | SER195 |
A | ALA196 |
A | ALA198 |
A | SER228 |
A | GLN252 |
A | TYR254 |
A | THR280 |
A | LYS349 |
A | SER371 |
A | HIS373 |
A | GLY374 |
A | ARG376 |
A | ASP409 |
A | GLY410 |
A | GLY411 |
A | ARG413 |
A | GLY432 |
A | ARG433 |
A | LEU436 |
A | SO3580 |
A | HOH615 |
A | HOH623 |
site_id | AC4 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEM A 560 |
Chain | Residue |
A | PHE39 |
A | HIS43 |
A | PRO44 |
A | GLY45 |
A | VAL49 |
A | ILE50 |
A | VAL58 |
A | ILE61 |
A | PHE62 |
A | HIS66 |
A | ILE71 |
A | ILE75 |
A | TYR97 |
A | GLN139 |
A | TYR143 |
A | ALA198 |
A | LEU199 |
A | LEU230 |
A | LYS296 |
site_id | AC5 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE FMN B 570 |
Chain | Residue |
B | TYR144 |
B | SER195 |
B | ALA196 |
B | ALA198 |
B | SER228 |
B | GLN252 |
B | TYR254 |
B | THR280 |
B | LYS349 |
B | SER371 |
B | HIS373 |
B | GLY374 |
B | ARG376 |
B | ASP409 |
B | GLY410 |
B | GLY411 |
B | ARG413 |
B | GLY432 |
B | ARG433 |
B | LEU436 |
B | SO3580 |
B | HOH746 |
B | HOH747 |
Functional Information from PROSITE/UniProt
site_id | PS00191 |
Number of Residues | 8 |
Details | CYTOCHROME_B5_1 Cytochrome b5 family, heme-binding domain signature. FLPNHPGG |
Chain | Residue | Details |
A | PHE39-GLY46 | |
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 | SER371-GLN377 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS373 | |
B | HIS373 | |
Chain | Residue | Details |
A | HIS43 | |
A | HIS66 | |
B | HIS43 | |
B | HIS66 | |
Chain | Residue | Details |
A | TYR97 | |
A | ARG376 | |
A | ASP409 | |
A | GLY432 | |
B | TYR97 | |
B | TYR143 | |
B | SER195 | |
B | SER228 | |
B | GLN252 | |
B | TYR254 | |
B | THR280 | |
A | TYR143 | |
B | LYS349 | |
B | HIS373 | |
B | ARG376 | |
B | ASP409 | |
B | GLY432 | |
A | SER195 | |
A | SER228 | |
A | GLN252 | |
A | TYR254 | |
A | THR280 | |
A | LYS349 | |
A | HIS373 | |
Chain | Residue | Details |
A | GLN139 | |
A | LYS296 | |
B | GLN139 | |
B | LYS296 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1fcb |
Chain | Residue | Details |
A | TYR254 | |
A | TYR143 | |
A | ARG376 | |
A | ASP282 | |
A | HIS373 | |
site_id | CSA2 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1fcb |
Chain | Residue | Details |
B | TYR254 | |
B | TYR143 | |
B | ARG376 | |
B | ASP282 | |
B | HIS373 | |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1fcb |
Chain | Residue | Details |
A | TYR254 | |
A | ARG376 | |
A | HIS373 | |
A | ASP282 | |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1fcb |
Chain | Residue | Details |
B | TYR254 | |
B | ARG376 | |
B | HIS373 | |
B | ASP282 | |
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 102 |
Chain | Residue | Details |
A | TYR254 | electrostatic stabiliser, hydrogen bond donor |
A | ASP282 | electrostatic stabiliser, hydrogen bond acceptor |
A | HIS373 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 102 |
Chain | Residue | Details |
B | TYR254 | electrostatic stabiliser, hydrogen bond donor |
B | ASP282 | electrostatic stabiliser, hydrogen bond acceptor |
B | HIS373 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |