3B5Q
Crystal structure of a putative sulfatase (NP_810509.1) from Bacteroides thetaiotaomicron VPI-5482 at 2.40 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004065 | molecular_function | arylsulfatase activity |
| A | 0015024 | molecular_function | glucuronate-2-sulfatase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004065 | molecular_function | arylsulfatase activity |
| B | 0015024 | molecular_function | glucuronate-2-sulfatase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 500 |
| Chain | Residue |
| A | CYS225 |
| A | CYS226 |
| A | HIS462 |
| A | HIS469 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 500 |
| Chain | Residue |
| B | CYS225 |
| B | CYS226 |
| B | HIS462 |
| B | HIS469 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL A 501 |
| Chain | Residue |
| A | GLU378 |
| A | TYR379 |
| A | GLU380 |
| A | TYR381 |
| A | VAL382 |
| A | SER377 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 501 |
| Chain | Residue |
| B | GLU378 |
| B | TYR379 |
| B | GLU380 |
| B | TYR381 |
| B | VAL382 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EPE B 502 |
| Chain | Residue |
| A | ARG393 |
| A | LYS411 |
| B | GLU204 |
| B | LEU205 |
| B | PRO206 |
| B | ASP207 |
| B | PHE209 |
| B | ASP210 |
| B | ARG417 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EPE B 503 |
| Chain | Residue |
| A | LYS412 |
| B | GLU212 |
| B | ASP213 |
| B | TRP214 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE EPE B 504 |
| Chain | Residue |
| B | SER64 |
| B | ASN85 |
| B | LYS117 |
| B | HIS119 |
| B | HIS180 |
| B | CYS183 |
| B | ARG229 |
| B | ARG230 |
| B | LYS296 |
| B | GLU378 |
| B | TYR379 |
| B | HOH547 |
| B | HOH611 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 502 |
| Chain | Residue |
| A | PHE137 |
| A | THR138 |
| A | PHE149 |
| A | TYR268 |
| A | HOH563 |
| A | HOH664 |
| A | HOH691 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 503 |
| Chain | Residue |
| A | LEU327 |
| A | THR328 |
| A | ASP333 |
| A | ILE353 |
| A | LEU355 |
| A | SER367 |
| A | HIS368 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 504 |
| Chain | Residue |
| A | GLY39 |
| A | CYS40 |
| A | THR41 |
| A | LEU42 |
| A | LYS258 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 505 |
| Chain | Residue |
| B | LEU327 |
| B | THR328 |
| B | ASP333 |
| B | LEU355 |
| B | SER367 |
| B | HIS368 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 505 |
| Chain | Residue |
| A | LYS412 |
| B | ASP210 |
| B | TRP214 |
| B | ARG292 |
| site_id | BC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 506 |
| Chain | Residue |
| A | SER49 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 506 |
| Chain | Residue |
| B | ILE217 |
| B | PRO218 |
| B | GLU405 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 507 |
| Chain | Residue |
| A | VAL211 |
| A | GLU212 |
| A | ASP213 |
| A | ILE217 |
| A | ARG417 |
| A | LYS418 |
| A | ASN419 |
| A | HOH553 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 507 |
| Chain | Residue |
| B | LEU326 |
| B | LEU327 |
| B | SER367 |
| B | HIS368 |
| B | EDO512 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 508 |
| Chain | Residue |
| A | ARG29 |
| A | THR37 |
| A | ILE246 |
| A | GLN250 |
| A | MSE288 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 508 |
| Chain | Residue |
| B | HIS469 |
| B | GLU470 |
| B | GLY471 |
| B | PRO472 |
| B | GLY473 |
| B | CYS226 |
| B | ARG458 |
| B | CYS459 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 509 |
| Chain | Residue |
| A | PRO89 |
| A | ASN91 |
| A | THR92 |
| B | ARG393 |
| B | TYR394 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 510 |
| Chain | Residue |
| A | ALA134 |
| A | LYS135 |
| A | PRO136 |
| A | ARG274 |
| A | PRO314 |
| A | HOH596 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 511 |
| Chain | Residue |
| A | ILE217 |
| A | PRO218 |
| A | GLY404 |
| A | GLU405 |
| A | LYS422 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 512 |
| Chain | Residue |
| A | ASP139 |
| A | PRO140 |
| A | GLU141 |
| A | ARG196 |
| A | LYS265 |
| site_id | CC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 509 |
| Chain | Residue |
| B | HIS251 |
| B | LYS254 |
| B | LYS258 |
| site_id | CC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 510 |
| Chain | Residue |
| B | ASP139 |
| B | ARG196 |
| B | LYS265 |
| B | HOH692 |
| site_id | CC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO B 511 |
| Chain | Residue |
| B | LYS128 |
| site_id | CC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 512 |
| Chain | Residue |
| B | ASP324 |
| B | PRO392 |
| B | EDO507 |
| B | EDO513 |
| site_id | CC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 513 |
| Chain | Residue |
| B | ARG390 |
| B | PRO392 |
| B | EDO512 |
| site_id | DC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 513 |
| Chain | Residue |
| B | ARG292 |
| site_id | DC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 514 |
| Chain | Residue |
| A | LYS365 |
| B | ASP454 |
| B | ASP456 |
| B | HOH694 |
| site_id | DC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 514 |
| Chain | Residue |
| A | GLN28 |
| A | ARG29 |
| A | GLN36 |
| A | HOH700 |
| site_id | DC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 515 |
| Chain | Residue |
| A | HIS251 |
| A | LYS254 |
| A | LYS258 |
| site_id | DC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 515 |
| Chain | Residue |
| B | ALA134 |
| B | LYS135 |
| B | ARG274 |
| B | GLY313 |
| B | PRO314 |
| B | HOH693 |
| site_id | DC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEG B 516 |
| Chain | Residue |
| B | PRO43 |
| B | GLU46 |
| B | ARG50 |
| B | PHE137 |
| B | THR138 |
| B | VAL144 |
| B | TYR268 |
| site_id | DC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG B 517 |
| Chain | Residue |
| B | LYS15 |
| B | SER108 |
| B | TYR110 |
| B | PRO169 |
| B | ALA342 |
| site_id | DC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG A 516 |
| Chain | Residue |
| A | LYS15 |
| A | SER108 |
| A | PRO169 |
| A | ALA342 |
| A | GLY343 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of a putative sulfatase (NP_810509.1) from Bacteroides thetaiotaomicron VPI-5482 at 2.40 A resolution.","authoringGroup":["Joint Center for Structural Genomics (JCSG)"]}},{"source":"PDB","id":"3B5Q","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"3-oxoalanine (Ser)","evidences":[{"source":"UniProtKB","id":"Q9X759","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
