3KTC
Crystal structure of Putative sugar isomerase (YP_050048.1) from ERWINIA CAROTOVORA ATROSEPTICA SCRI1043 at 1.54 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0009045 | molecular_function | xylose isomerase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0009045 | molecular_function | xylose isomerase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 333 |
| Chain | Residue |
| A | ASP201 |
| A | HIS204 |
| A | ASP238 |
| A | ASP240 |
| A | HOH734 |
| B | HOH733 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE A 334 |
| Chain | Residue |
| A | ASP270 |
| A | GLU166 |
| A | ASP201 |
| A | ASP229 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 335 |
| Chain | Residue |
| A | HOH511 |
| A | HOH511 |
| A | HOH528 |
| A | HOH531 |
| A | HOH531 |
| A | HOH599 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 336 |
| Chain | Residue |
| A | GLY223 |
| A | LEU225 |
| A | HOH458 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 339 |
| Chain | Residue |
| A | TRP132 |
| A | LYS175 |
| A | MSE176 |
| A | THR177 |
| A | ARG183 |
| A | HOH538 |
| A | HOH610 |
| B | ASP214 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 340 |
| Chain | Residue |
| A | PRO159 |
| A | ASP160 |
| A | LYS162 |
| A | ASN195 |
| A | HOH595 |
| A | HOH707 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 341 |
| Chain | Residue |
| A | ILE77 |
| A | ASN121 |
| A | PHE226 |
| A | GLY227 |
| A | GLY265 |
| A | VAL266 |
| A | HOH399 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 342 |
| Chain | Residue |
| A | GLU210 |
| A | SER211 |
| A | ASP214 |
| A | SER215 |
| A | HOH446 |
| B | ASP179 |
| B | ARG183 |
| B | EDO341 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 343 |
| Chain | Residue |
| A | TYR28 |
| A | SER89 |
| A | ARG90 |
| A | PHE274 |
| A | HOH539 |
| A | HOH613 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 344 |
| Chain | Residue |
| A | ILE260 |
| A | ASN261 |
| A | HOH525 |
| A | HOH617 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B 333 |
| Chain | Residue |
| A | HOH734 |
| B | ASP201 |
| B | HIS204 |
| B | ASP238 |
| B | ASP240 |
| B | HOH733 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE B 334 |
| Chain | Residue |
| B | GLU166 |
| B | ASP201 |
| B | ASP229 |
| B | ASP270 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MG B 335 |
| Chain | Residue |
| B | HOH363 |
| B | HOH363 |
| B | HOH402 |
| B | HOH402 |
| B | HOH405 |
| B | HOH405 |
| B | HOH434 |
| B | HOH434 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 336 |
| Chain | Residue |
| B | GLY223 |
| B | LEU225 |
| B | HOH381 |
| B | HOH653 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 338 |
| Chain | Residue |
| B | GLU189 |
| B | ARG222 |
| B | ARG224 |
| B | HOH539 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 339 |
| Chain | Residue |
| A | LYS141 |
| A | HOH589 |
| B | GLN217 |
| B | ILE260 |
| B | ASN261 |
| B | HOH559 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 340 |
| Chain | Residue |
| B | PRO159 |
| B | ASP160 |
| B | LYS162 |
| B | ASN195 |
| B | HOH421 |
| B | HOH668 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 341 |
| Chain | Residue |
| B | MSE176 |
| B | THR177 |
| B | ARG183 |
| B | HOH579 |
| B | HOH612 |
| A | EDO342 |
| B | TRP132 |
| B | LYS175 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 342 |
| Chain | Residue |
| B | TYR28 |
| B | SER89 |
| B | ARG90 |
| B | PHE274 |
| B | HOH398 |
| B | HOH625 |
| site_id | CC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO B 343 |
| Chain | Residue |
| B | ILE77 |
| B | ASN121 |
| B | PHE226 |
| B | GLY227 |
| B | GLY265 |
| B | VAL266 |
| B | HOH368 |
| B | HOH617 |
| B | HOH700 |
| site_id | CC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO B 344 |
| Chain | Residue |
| A | GLN308 |
| A | GLU309 |
| A | GLN311 |
| A | HOH375 |
| A | HOH435 |
| B | VAL138 |
| B | SER139 |
| B | ASN142 |
| B | LEU143 |
| B | HOH530 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 345 |
| Chain | Residue |
| B | GLY45 |
| B | LEU47 |
| B | SER48 |
| B | HOH511 |
| B | HOH654 |
| site_id | CC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 346 |
| Chain | Residue |
| B | LEU13 |
| B | THR34 |
| B | LEU52 |
| B | PRO53 |
| B | PHE56 |
| B | HOH618 |
| B | HOH637 |
| B | HOH676 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of putative sugar isomerase (YP_050048.1) from Erwinia carotovora atroseptica SCRI1043 at 1.54 A resolution.","authoringGroup":["Joint Center for Structural Genomics (JCSG)"]}}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| A | HIS204 | |
| A | ASP238 | |
| A | LYS168 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1de6 |
| Chain | Residue | Details |
| B | HIS204 | |
| B | ASP238 | |
| B | LYS168 |
