4RPK
Crystal structure of Micobacterium tuberculosis UDP-Galactopyranose mutase in complex with tetrafluorinated substrate analog UDP-F4-Galf
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
A | 0009274 | cellular_component | peptidoglycan-based cell wall |
A | 0016853 | molecular_function | isomerase activity |
A | 0045227 | biological_process | capsule polysaccharide biosynthetic process |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0071555 | biological_process | cell wall organization |
A | 0071766 | biological_process | Actinobacterium-type cell wall biogenesis |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
B | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
B | 0009274 | cellular_component | peptidoglycan-based cell wall |
B | 0016853 | molecular_function | isomerase activity |
B | 0045227 | biological_process | capsule polysaccharide biosynthetic process |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0071555 | biological_process | cell wall organization |
B | 0071766 | biological_process | Actinobacterium-type cell wall biogenesis |
C | 0005829 | cellular_component | cytosol |
C | 0005886 | cellular_component | plasma membrane |
C | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
C | 0009274 | cellular_component | peptidoglycan-based cell wall |
C | 0016853 | molecular_function | isomerase activity |
C | 0045227 | biological_process | capsule polysaccharide biosynthetic process |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
C | 0071555 | biological_process | cell wall organization |
C | 0071766 | biological_process | Actinobacterium-type cell wall biogenesis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE FAD B 401 |
Chain | Residue |
B | GLY14 |
B | ASN46 |
B | TYR62 |
B | ALA64 |
B | HIS65 |
B | LEU66 |
B | THR223 |
B | ASP224 |
B | TRP225 |
B | GLY245 |
B | ARG249 |
B | GLY16 |
B | LEU263 |
B | TYR327 |
B | TYR328 |
B | GLY359 |
B | ARG360 |
B | LEU367 |
B | ASP368 |
B | MET369 |
B | 3UA402 |
B | HOH505 |
B | PHE17 |
B | HOH536 |
B | HOH548 |
B | HOH570 |
B | HOH572 |
B | HOH600 |
B | PHE18 |
B | LEU37 |
B | GLU38 |
B | ARG39 |
B | ARG40 |
B | GLY45 |
site_id | AC2 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE 3UA B 402 |
Chain | Residue |
B | ALA64 |
B | LEU66 |
B | HIS89 |
B | VAL91 |
B | PHE102 |
B | PHE157 |
B | VAL158 |
B | TYR161 |
B | THR162 |
B | GLN165 |
B | TRP166 |
B | ASN177 |
B | ARG180 |
B | LEU181 |
B | TYR191 |
B | VAL280 |
B | ASN282 |
B | ASN284 |
B | ARG292 |
B | TYR328 |
B | TYR366 |
B | FAD401 |
B | HOH517 |
B | HOH549 |
B | HOH551 |
B | HOH586 |
B | HOH587 |
site_id | AC3 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE FAD A 401 |
Chain | Residue |
A | VAL13 |
A | GLY14 |
A | GLY16 |
A | PHE17 |
A | PHE18 |
A | LEU37 |
A | GLU38 |
A | ARG39 |
A | ARG40 |
A | GLY45 |
A | TYR62 |
A | ALA64 |
A | HIS65 |
A | LEU66 |
A | THR223 |
A | ASP224 |
A | TRP225 |
A | PHE226 |
A | GLY245 |
A | ARG249 |
A | LEU263 |
A | TYR327 |
A | TYR328 |
A | GLY359 |
A | ARG360 |
A | LEU367 |
A | ASP368 |
A | MET369 |
A | 3UA402 |
A | HOH505 |
A | HOH559 |
A | HOH560 |
A | HOH563 |
A | HOH564 |
A | HOH577 |
site_id | AC4 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE 3UA A 402 |
Chain | Residue |
A | VAL91 |
A | PHE102 |
A | PHE157 |
A | VAL158 |
A | TYR161 |
A | THR162 |
A | GLN165 |
A | TRP166 |
A | ASN177 |
A | ARG180 |
A | LEU181 |
A | TYR191 |
A | VAL280 |
A | ASN282 |
A | ASN284 |
A | ARG292 |
A | TYR328 |
A | TYR366 |
A | FAD401 |
A | HOH529 |
A | HOH561 |
A | HOH578 |
A | HOH579 |
A | HOH607 |
A | ALA64 |
A | LEU66 |
A | HIS89 |
site_id | AC5 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE FAD C 401 |
Chain | Residue |
C | VAL13 |
C | GLY14 |
C | GLY16 |
C | PHE17 |
C | LEU37 |
C | GLU38 |
C | ARG39 |
C | ARG40 |
C | GLY45 |
C | ASN46 |
C | TYR62 |
C | ALA64 |
C | HIS65 |
C | LEU66 |
C | THR223 |
C | ASP224 |
C | TRP225 |
C | PHE226 |
C | GLY245 |
C | LEU263 |
C | TYR327 |
C | TYR328 |
C | GLY359 |
C | ARG360 |
C | LEU367 |
C | ASP368 |
C | MET369 |
C | ALA372 |
C | 3UA402 |
C | HOH502 |
C | HOH505 |
C | HOH555 |
C | HOH556 |
C | HOH574 |
site_id | AC6 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE 3UA C 402 |
Chain | Residue |
C | ALA64 |
C | LEU66 |
C | HIS89 |
C | VAL91 |
C | PHE102 |
C | PHE157 |
C | VAL158 |
C | TYR161 |
C | THR162 |
C | TRP166 |
C | ASN177 |
C | ILE178 |
C | ARG180 |
C | LEU181 |
C | TYR191 |
C | ASN282 |
C | ASN284 |
C | ARG292 |
C | TYR328 |
C | TYR366 |
C | FAD401 |
C | HOH549 |
C | HOH584 |
C | HOH585 |
C | HOH597 |
C | HOH598 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 21 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15843027 |
Chain | Residue | Details |
B | PHE18 | |
A | ASN46 | |
A | LEU66 | |
A | ASP224 | |
A | ARG360 | |
A | LEU367 | |
C | PHE18 | |
C | GLU38 | |
C | ASN46 | |
C | LEU66 | |
C | ASP224 | |
B | GLU38 | |
C | ARG360 | |
C | LEU367 | |
B | ASN46 | |
B | LEU66 | |
B | ASP224 | |
B | ARG360 | |
B | LEU367 | |
A | PHE18 | |
A | GLU38 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
B | PHE157 | |
A | THR162 | |
A | TRP166 | |
A | TYR191 | |
A | ASN282 | |
A | ARG292 | |
A | TYR328 | |
A | TYR366 | |
C | PHE157 | |
C | THR162 | |
C | TRP166 | |
B | THR162 | |
C | TYR191 | |
C | ASN282 | |
C | ARG292 | |
C | TYR328 | |
C | TYR366 | |
B | TRP166 | |
B | TYR191 | |
B | ASN282 | |
B | ARG292 | |
B | TYR328 | |
B | TYR366 | |
A | PHE157 |