4DOY
Crystal structure of Dibenzothiophene desulfurization enzyme C
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0018896 | biological_process | dibenzothiophene catabolic process |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0018896 | biological_process | dibenzothiophene catabolic process |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| C | 0018896 | biological_process | dibenzothiophene catabolic process |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| D | 0018896 | biological_process | dibenzothiophene catabolic process |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0004497 | molecular_function | monooxygenase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| E | 0018896 | biological_process | dibenzothiophene catabolic process |
| E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0004497 | molecular_function | monooxygenase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| F | 0018896 | biological_process | dibenzothiophene catabolic process |
| F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0004497 | molecular_function | monooxygenase activity |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| G | 0018896 | biological_process | dibenzothiophene catabolic process |
| G | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0004497 | molecular_function | monooxygenase activity |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| H | 0018896 | biological_process | dibenzothiophene catabolic process |
| H | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 500 |
| Chain | Residue |
| A | LEU61 |
| A | ALA71 |
| A | ASP72 |
| A | GLN324 |
| A | HOH718 |
| A | HOH794 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL B 501 |
| Chain | Residue |
| B | TRP73 |
| B | GLN324 |
| B | TRP327 |
| B | HOH665 |
| B | HOH728 |
| B | HOH779 |
| B | HOH833 |
| B | HOH945 |
| B | LEU61 |
| B | ALA71 |
| B | ASP72 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 502 |
| Chain | Residue |
| B | TRP205 |
| B | HIS391 |
| B | HOH744 |
| E | ALA369 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 500 |
| Chain | Residue |
| C | LEU61 |
| C | ALA71 |
| C | ASP72 |
| C | GLN324 |
| C | HOH790 |
| C | HOH809 |
| C | HOH931 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D 501 |
| Chain | Residue |
| D | ASP72 |
| D | GLN324 |
| D | GOL502 |
| D | HOH804 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 502 |
| Chain | Residue |
| D | LEU61 |
| D | ALA71 |
| D | TRP73 |
| D | GOL501 |
| D | HOH913 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL E 501 |
| Chain | Residue |
| E | LEU61 |
| E | ALA71 |
| E | ASP72 |
| E | TRP73 |
| E | GLN324 |
| E | HOH762 |
| E | HOH798 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL E 502 |
| Chain | Residue |
| E | TRP205 |
| E | THR387 |
| E | HOH796 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL F 500 |
| Chain | Residue |
| F | LEU61 |
| F | ALA71 |
| F | ASP72 |
| F | TRP73 |
| F | GLN324 |
| F | TRP327 |
| F | HOH792 |
| F | HOH863 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL G 501 |
| Chain | Residue |
| G | LEU61 |
| G | ALA71 |
| G | ASP72 |
| G | TRP73 |
| G | GLN324 |
| G | TRP327 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL G 502 |
| Chain | Residue |
| G | TRP205 |
| G | THR387 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL H 501 |
| Chain | Residue |
| H | LEU61 |
| H | ALA71 |
| H | TRP73 |
| H | GLN324 |
| H | TRP327 |
| site_id | BC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL H 502 |
| Chain | Residue |
| H | TRP205 |
Functional Information from PROSITE/UniProt
| site_id | PS00962 |
| Number of Residues | 12 |
| Details | RIBOSOMAL_S2_1 Ribosomal protein S2 signature 1. IaQLIFANVYLG |
| Chain | Residue | Details |
| A | ILE253-GLY264 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:24470304 |
| Chain | Residue | Details |
| A | HIS92 | |
| D | HIS92 | |
| D | ASN129 | |
| D | TRP205 | |
| E | HIS92 | |
| E | ASN129 | |
| E | TRP205 | |
| F | HIS92 | |
| F | ASN129 | |
| F | TRP205 | |
| G | HIS92 | |
| A | ASN129 | |
| G | ASN129 | |
| G | TRP205 | |
| H | HIS92 | |
| H | ASN129 | |
| H | TRP205 | |
| A | TRP205 | |
| B | HIS92 | |
| B | ASN129 | |
| B | TRP205 | |
| C | HIS92 | |
| C | ASN129 | |
| C | TRP205 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:A0A0C6DRW4, ECO:0000305|PubMed:24470304 |
| Chain | Residue | Details |
| A | TYR96 | |
| C | LYS159 | |
| C | ARG282 | |
| C | ALA369 | |
| D | TYR96 | |
| D | LYS159 | |
| D | ARG282 | |
| D | ALA369 | |
| E | TYR96 | |
| E | LYS159 | |
| E | ARG282 | |
| A | LYS159 | |
| E | ALA369 | |
| F | TYR96 | |
| F | LYS159 | |
| F | ARG282 | |
| F | ALA369 | |
| G | TYR96 | |
| G | LYS159 | |
| G | ARG282 | |
| G | ALA369 | |
| H | TYR96 | |
| A | ARG282 | |
| H | LYS159 | |
| H | ARG282 | |
| H | ALA369 | |
| A | ALA369 | |
| B | TYR96 | |
| B | LYS159 | |
| B | ARG282 | |
| B | ALA369 | |
| C | TYR96 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:A0A0C6DRW4 |
| Chain | Residue | Details |
| A | HIS391 | |
| B | HIS391 | |
| C | HIS391 | |
| D | HIS391 | |
| E | HIS391 | |
| F | HIS391 | |
| G | HIS391 | |
| H | HIS391 |
