1A0C
XYLOSE ISOMERASE FROM THERMOANAEROBACTERIUM THERMOSULFURIGENES
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
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 | 0042732 | biological_process | D-xylose metabolic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0000287 | molecular_function | magnesium 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 | 0042732 | biological_process | D-xylose metabolic process |
B | 0046872 | molecular_function | metal ion binding |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005975 | biological_process | carbohydrate metabolic process |
C | 0009045 | molecular_function | xylose isomerase activity |
C | 0016853 | molecular_function | isomerase activity |
C | 0042732 | biological_process | D-xylose metabolic process |
C | 0046872 | molecular_function | metal ion binding |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005975 | biological_process | carbohydrate metabolic process |
D | 0009045 | molecular_function | xylose isomerase activity |
D | 0016853 | molecular_function | isomerase activity |
D | 0042732 | biological_process | D-xylose metabolic process |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CO A 491 |
Chain | Residue |
A | GLU231 |
A | GLU267 |
A | ASP295 |
A | ASP338 |
A | HOH494 |
A | HOH495 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CO A 492 |
Chain | Residue |
A | GLU267 |
A | HIS270 |
A | ASP306 |
A | ASP308 |
A | HOH493 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CO B 491 |
Chain | Residue |
B | GLU231 |
B | GLU267 |
B | ASP295 |
B | ASP338 |
B | HOH527 |
B | HOH528 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CO B 492 |
Chain | Residue |
B | GLU267 |
B | HIS270 |
B | ASP306 |
B | ASP308 |
B | HOH526 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CO C 491 |
Chain | Residue |
C | GLU231 |
C | GLU267 |
C | ASP295 |
C | ASP338 |
C | HOH525 |
C | HOH526 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CO C 492 |
Chain | Residue |
C | GLU267 |
C | HIS270 |
C | ASP306 |
C | ASP308 |
C | HOH524 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CO D 491 |
Chain | Residue |
D | GLU231 |
D | GLU267 |
D | ASP295 |
D | ASP338 |
D | HOH558 |
D | HOH559 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CO D 492 |
Chain | Residue |
D | GLU267 |
D | HIS270 |
D | ASP306 |
D | ASP308 |
D | HOH557 |
site_id | CO1 |
Number of Residues | 6 |
Details | CO BINDING SITE 1 OF MOLECULE A |
Chain | Residue |
A | GLU231 |
A | GLU267 |
A | ASP295 |
A | ASP338 |
A | HOH494 |
A | HOH495 |
site_id | CO2 |
Number of Residues | 5 |
Details | CO BINDING SITE 2 OF MOLECULE A |
Chain | Residue |
A | ASP308 |
A | HOH493 |
A | GLU267 |
A | HIS270 |
A | ASP306 |
site_id | CO3 |
Number of Residues | 6 |
Details | CO BINDING SITE 1 OF MOLECULE B |
Chain | Residue |
B | GLU231 |
B | GLU267 |
B | ASP295 |
B | ASP338 |
B | HOH527 |
B | HOH528 |
site_id | CO4 |
Number of Residues | 5 |
Details | CO BINDING SITE 2 OF MOLECULE B |
Chain | Residue |
B | GLU267 |
B | HIS270 |
B | ASP306 |
B | ASP308 |
B | HOH526 |
site_id | CO5 |
Number of Residues | 6 |
Details | CO BINDING SITE 1 OF MOLECULE C |
Chain | Residue |
C | GLU231 |
C | GLU267 |
C | ASP295 |
C | ASP338 |
C | HOH525 |
C | HOH526 |
site_id | CO6 |
Number of Residues | 5 |
Details | CO BINDING SITE 2 OF MOLECULE C |
Chain | Residue |
C | GLU267 |
C | HIS270 |
C | ASP306 |
C | ASP308 |
C | HOH524 |
site_id | CO7 |
Number of Residues | 6 |
Details | CO BINDING SITE 1 OF MOLECULE D |
Chain | Residue |
D | GLU231 |
D | GLU267 |
D | ASP295 |
D | ASP338 |
D | HOH558 |
D | HOH559 |
site_id | CO8 |
Number of Residues | 5 |
Details | CO BINDING SITE 2 OF MOLECULE D |
Chain | Residue |
D | GLU267 |
D | HIS270 |
D | ASP306 |
D | ASP308 |
D | HOH557 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: |
Chain | Residue | Details |
A | HIS100 | |
B | HIS100 | |
C | HIS100 | |
D | HIS100 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000250 |
Chain | Residue | Details |
A | ASP103 | |
B | ASP103 | |
C | ASP103 | |
D | ASP103 |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | BINDING: |
Chain | Residue | Details |
A | GLU231 | |
B | HIS270 | |
B | ASP295 | |
B | ASP306 | |
B | ASP308 | |
B | ASP338 | |
C | GLU231 | |
C | GLU267 | |
C | HIS270 | |
C | ASP295 | |
C | ASP306 | |
A | GLU267 | |
C | ASP308 | |
C | ASP338 | |
D | GLU231 | |
D | GLU267 | |
D | HIS270 | |
D | ASP295 | |
D | ASP306 | |
D | ASP308 | |
D | ASP338 | |
A | HIS270 | |
A | ASP295 | |
A | ASP306 | |
A | ASP308 | |
A | ASP338 | |
B | GLU231 | |
B | GLU267 |