4DMR
REDUCED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS WITH BOUND DMSO SUBSTRATE
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE PGD A 782 |
| Chain | Residue |
| A | GLY432 |
| A | GLY433 |
| A | ASN434 |
| A | HIS438 |
| A | GLN440 |
| A | HIS458 |
| A | ASP459 |
| A | PHE460 |
| A | THR463 |
| A | ALA475 |
| A | TYR114 |
| A | ARG481 |
| A | ASP511 |
| A | ALA641 |
| A | HIS643 |
| A | HIS649 |
| A | SER650 |
| A | GLN651 |
| A | GLU715 |
| A | ASN737 |
| A | GLY754 |
| A | GLY115 |
| A | GLN755 |
| A | PGD783 |
| A | 4MO784 |
| A | O785 |
| A | DMS786 |
| A | HOH799 |
| A | HOH814 |
| A | HOH832 |
| A | HOH840 |
| A | TRP116 |
| A | LYS117 |
| A | SER118 |
| A | TYR146 |
| A | SER147 |
| A | ARG326 |
| site_id | AC2 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE PGD A 783 |
| Chain | Residue |
| A | TRP116 |
| A | SER147 |
| A | ALA185 |
| A | LYS190 |
| A | THR191 |
| A | GLN193 |
| A | ILE194 |
| A | ILE220 |
| A | ASP221 |
| A | PRO222 |
| A | VAL223 |
| A | THR225 |
| A | PRO240 |
| A | GLN241 |
| A | ASP243 |
| A | GLY321 |
| A | TRP322 |
| A | SER323 |
| A | ARG326 |
| A | MET327 |
| A | HIS359 |
| A | SER642 |
| A | HIS643 |
| A | PRO644 |
| A | PHE645 |
| A | ARG647 |
| A | LEU648 |
| A | HIS649 |
| A | GLN755 |
| A | PGD782 |
| A | 4MO784 |
| A | O785 |
| A | DMS786 |
| A | HOH801 |
| A | HOH813 |
| A | HOH824 |
| A | HOH854 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 4MO A 784 |
| Chain | Residue |
| A | SER147 |
| A | PGD782 |
| A | PGD783 |
| A | O785 |
| A | DMS786 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE O A 785 |
| Chain | Residue |
| A | TYR114 |
| A | SER147 |
| A | PGD782 |
| A | PGD783 |
| A | 4MO784 |
| A | DMS786 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE DMS A 786 |
| Chain | Residue |
| A | TYR114 |
| A | TRP116 |
| A | SER147 |
| A | TRP196 |
| A | TYR360 |
| A | PGD782 |
| A | PGD783 |
| A | 4MO784 |
| A | O785 |
| site_id | MO |
| Number of Residues | 1 |
| Details | THE SUBSTRATE DMSO IS BOUND AT THE ACTIVE SITE TO THE MOLYBDENUM, WHICH IS IN THE REDUCED (+4) STATE. THE MOLYBDENUM IS COORDINATED BY THE PTERIN SULFURS AND ANOTHER SINGLE OXYGEN. |
| Chain | Residue |
| A | SER147 |
Functional Information from PROSITE/UniProt
| site_id | PS00490 |
| Number of Residues | 18 |
| Details | MOLYBDOPTERIN_PROK_2 Prokaryotic molybdopterin oxidoreductases signature 2. TpTArhADIVLPaTTsyE |
| Chain | Residue | Details |
| A | THR463-GLU480 |
| site_id | PS00932 |
| Number of Residues | 28 |
| Details | MOLYBDOPTERIN_PROK_3 Prokaryotic molybdopterin oxidoreductases signature 3. AaarGIaDgDvVrVhNdrGqiltgVkVT |
| Chain | Residue | Details |
| A | ALA676-THR703 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 15 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10835270","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10985771","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11502174","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8890912","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9466935","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1997","firstPage":"690","lastPage":"700","volume":"2","journal":"J. Biol. Inorg. Chem.","title":"Molybdenum active centre of DMSO reductase from Rhodobacter capsulatus: crystal structure of the oxidised enzyme at 1.82-A resolution and the dithionite-reduced enzyme at 2.8-A resolution.","authors":["McAlpine A.S.","McEwan A.G.","Shaw A.L.","Bailey S."]}}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tmo |
| Chain | Residue | Details |
| A | SER147 |
