4RPG
Crystal structure of Micobacterium tuberculosis UDP-Galactopyranose mutase in complex with substrate UDP-Galp
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 | 37 |
| Details | BINDING SITE FOR RESIDUE FAD B 401 |
| Chain | Residue |
| B | VAL13 |
| B | GLY45 |
| B | ASN46 |
| B | TYR62 |
| B | ALA64 |
| B | HIS65 |
| B | LEU66 |
| B | THR223 |
| B | ASP224 |
| B | TRP225 |
| B | PHE226 |
| B | GLY14 |
| B | THR244 |
| B | GLY245 |
| B | LEU263 |
| B | TYR327 |
| B | TYR328 |
| B | GLY359 |
| B | ARG360 |
| B | LEU367 |
| B | ASP368 |
| B | MET369 |
| B | GLY16 |
| B | GDU402 |
| B | HOH505 |
| B | HOH507 |
| B | HOH510 |
| B | HOH605 |
| B | HOH619 |
| B | HOH639 |
| B | HOH648 |
| B | PHE17 |
| B | PHE18 |
| B | LEU37 |
| B | GLU38 |
| B | ARG39 |
| B | ARG40 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE GDU B 402 |
| Chain | Residue |
| B | LEU66 |
| B | HIS89 |
| B | VAL91 |
| B | PHE102 |
| B | PHE157 |
| B | VAL158 |
| B | TYR161 |
| B | THR162 |
| B | TRP166 |
| B | ASN177 |
| B | ARG180 |
| B | LEU181 |
| B | TYR191 |
| B | PHE192 |
| B | ASN282 |
| B | ASN284 |
| B | ARG292 |
| B | TYR328 |
| B | TYR366 |
| B | FAD401 |
| B | HOH509 |
| B | HOH513 |
| B | HOH544 |
| B | HOH553 |
| B | HOH591 |
| B | HOH619 |
| site_id | AC3 |
| Number of Residues | 34 |
| 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 | ASN46 |
| A | TYR62 |
| A | ALA64 |
| A | HIS65 |
| A | LEU66 |
| A | THR223 |
| A | ASP224 |
| A | TRP225 |
| A | PHE226 |
| A | GLY245 |
| A | LEU263 |
| A | TYR327 |
| A | TYR328 |
| A | GLY359 |
| A | ARG360 |
| A | LEU367 |
| A | ASP368 |
| A | MET369 |
| A | ALA372 |
| A | HOH501 |
| A | HOH506 |
| A | HOH516 |
| A | HOH630 |
| A | HOH632 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE UDP A 402 |
| Chain | Residue |
| A | PHE157 |
| A | VAL158 |
| A | TYR161 |
| A | THR162 |
| A | TRP166 |
| A | ASN177 |
| A | ARG180 |
| A | LEU181 |
| A | TYR191 |
| A | ASN282 |
| A | ASN284 |
| A | ARG292 |
| A | TYR328 |
| A | TYR366 |
| A | HOH510 |
| A | HOH521 |
| A | HOH579 |
| A | HOH629 |
| A | HOH633 |
| A | PHE102 |
| A | LEU141 |
| 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 | PHE18 |
| C | LEU37 |
| C | GLU38 |
| C | ARG39 |
| C | ARG40 |
| C | GLY45 |
| C | ASN46 |
| C | TYR62 |
| C | GLY63 |
| 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 | HOH504 |
| C | HOH505 |
| C | HOH520 |
| C | HOH555 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE UDP C 402 |
| Chain | Residue |
| 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 | HOH507 |
| C | HOH512 |
| C | HOH552 |
| C | HOH571 |
| C | HOH612 |
| C | HOH613 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15843027","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
