3HDY
Crystal Structure of UDP-galactopyranose mutase (reduced form) in complex with substrate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005829 | cellular_component | cytosol |
A | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0005829 | cellular_component | cytosol |
B | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0005829 | cellular_component | cytosol |
C | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
C | 0016853 | molecular_function | isomerase activity |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0005829 | cellular_component | cytosol |
D | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
D | 0016853 | molecular_function | isomerase activity |
D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
E | 0000166 | molecular_function | nucleotide binding |
E | 0005829 | cellular_component | cytosol |
E | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
E | 0016853 | molecular_function | isomerase activity |
E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
F | 0000166 | molecular_function | nucleotide binding |
F | 0005829 | cellular_component | cytosol |
F | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
F | 0016853 | molecular_function | isomerase activity |
F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
G | 0000166 | molecular_function | nucleotide binding |
G | 0005829 | cellular_component | cytosol |
G | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
G | 0016853 | molecular_function | isomerase activity |
G | 0050660 | molecular_function | flavin adenine dinucleotide binding |
H | 0000166 | molecular_function | nucleotide binding |
H | 0005829 | cellular_component | cytosol |
H | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
H | 0016853 | molecular_function | isomerase activity |
H | 0050660 | molecular_function | flavin adenine dinucleotide binding |
I | 0000166 | molecular_function | nucleotide binding |
I | 0005829 | cellular_component | cytosol |
I | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
I | 0016853 | molecular_function | isomerase activity |
I | 0050660 | molecular_function | flavin adenine dinucleotide binding |
J | 0000166 | molecular_function | nucleotide binding |
J | 0005829 | cellular_component | cytosol |
J | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
J | 0016853 | molecular_function | isomerase activity |
J | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE GDU A 500 |
Chain | Residue |
A | ILE86 |
A | THR196 |
A | ARG198 |
A | TYR209 |
A | PHE210 |
A | THR294 |
A | ASN296 |
A | ARG305 |
A | TYR335 |
A | TYR370 |
A | ASN372 |
A | HIS109 |
A | HOH401 |
A | HOH419 |
A | FAD450 |
A | VAL111 |
A | PHE175 |
A | PHE176 |
A | TYR179 |
A | THR180 |
A | TRP184 |
A | VAL195 |
site_id | AC2 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE FAD A 450 |
Chain | Residue |
A | VAL35 |
A | GLY36 |
A | GLY38 |
A | PHE39 |
A | ALA40 |
A | ASP59 |
A | ARG60 |
A | ARG61 |
A | GLY66 |
A | ASN67 |
A | TYR82 |
A | PRO84 |
A | HIS85 |
A | ILE86 |
A | HIS88 |
A | THR241 |
A | ASP242 |
A | TYR243 |
A | GLY259 |
A | LEU277 |
A | GLY363 |
A | ARG364 |
A | TYR371 |
A | ASN372 |
A | MET373 |
A | HOH398 |
A | HOH400 |
A | HOH404 |
A | HOH409 |
A | GDU500 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE GDU B 500 |
Chain | Residue |
B | HIS109 |
B | ILE122 |
B | PHE175 |
B | PHE176 |
B | TYR179 |
B | THR180 |
B | TRP184 |
B | VAL195 |
B | ARG198 |
B | TYR209 |
B | PHE210 |
B | ASN296 |
B | ARG305 |
B | TYR335 |
B | TYR370 |
B | ASN372 |
B | HOH405 |
B | HOH426 |
B | FDA1385 |
site_id | AC4 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE FDA B 1385 |
Chain | Residue |
B | VAL35 |
B | GLY36 |
B | GLY38 |
B | PHE39 |
B | ALA40 |
B | ASP59 |
B | ARG60 |
B | ARG61 |
B | GLY66 |
B | ASN67 |
B | TYR82 |
B | PRO84 |
B | HIS85 |
B | ILE86 |
B | THR241 |
B | ASP242 |
B | TYR243 |
B | GLY259 |
B | PRO260 |
B | LEU277 |
B | GLY363 |
B | ARG364 |
B | TYR371 |
B | ASN372 |
B | MET373 |
B | VAL376 |
B | HOH398 |
B | GDU500 |
site_id | AC5 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE FAD C 450 |
Chain | Residue |
C | GLY38 |
C | PHE39 |
C | ALA40 |
C | ASP59 |
C | ARG60 |
C | ARG61 |
C | GLY66 |
C | ASN67 |
C | TYR82 |
C | PRO84 |
C | HIS85 |
C | ILE86 |
C | THR241 |
C | ASP242 |
C | TYR243 |
C | ARG244 |
C | GLY259 |
C | LEU277 |
C | GLY363 |
C | ARG364 |
C | TYR371 |
C | ASN372 |
C | MET373 |
C | GDU500 |
site_id | AC6 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE GDU C 500 |
Chain | Residue |
C | ILE86 |
C | HIS109 |
C | PHE175 |
C | PHE176 |
C | TYR179 |
C | THR180 |
C | TRP184 |
C | VAL195 |
C | ARG198 |
C | TYR209 |
C | PHE210 |
C | ASN296 |
C | ARG305 |
C | TYR335 |
C | TYR370 |
C | HOH398 |
C | HOH405 |
C | FAD450 |
site_id | AC7 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE GDU D 500 |
Chain | Residue |
D | HIS109 |
D | PHE175 |
D | PHE176 |
D | TYR179 |
D | THR180 |
D | TRP184 |
D | VAL195 |
D | ARG198 |
D | TYR209 |
D | PHE210 |
D | ASN296 |
D | ARG305 |
D | TYR335 |
D | TYR370 |
D | ASN372 |
D | HOH422 |
D | HOH423 |
D | FDA1385 |
site_id | AC8 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE FDA D 1385 |
Chain | Residue |
D | VAL35 |
D | GLY36 |
D | GLY38 |
D | PHE39 |
D | ALA40 |
D | ASP59 |
D | ARG60 |
D | ARG61 |
D | GLY66 |
D | ASN67 |
D | TYR82 |
D | PRO84 |
D | HIS85 |
D | ILE86 |
D | ASP242 |
D | TYR243 |
D | THR258 |
D | LEU277 |
D | GLY363 |
D | ARG364 |
D | TYR371 |
D | ASN372 |
D | MET373 |
D | VAL376 |
D | HOH399 |
D | HOH401 |
D | GDU500 |
site_id | AC9 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE FAD E 450 |
Chain | Residue |
E | GLY36 |
E | GLY38 |
E | PHE39 |
E | ALA40 |
E | ASP59 |
E | ARG60 |
E | ARG61 |
E | GLY66 |
E | ASN67 |
E | TYR82 |
E | PRO84 |
E | HIS85 |
E | ILE86 |
E | HIS88 |
E | THR241 |
E | ASP242 |
E | TYR243 |
E | GLY259 |
E | LEU277 |
E | GLY363 |
E | ARG364 |
E | TYR371 |
E | ASN372 |
E | MET373 |
E | VAL376 |
E | HOH402 |
E | HOH404 |
E | HOH407 |
E | GDU500 |
site_id | BC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE GDU E 500 |
Chain | Residue |
E | HIS109 |
E | ILE122 |
E | PHE175 |
E | PHE176 |
E | TYR179 |
E | THR180 |
E | TRP184 |
E | VAL195 |
E | THR196 |
E | ARG198 |
E | TYR209 |
E | PHE210 |
E | THR294 |
E | ASN296 |
E | ARG305 |
E | TYR335 |
E | TYR370 |
E | ASN372 |
E | HOH405 |
E | FAD450 |
site_id | BC2 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE FAD F 450 |
Chain | Residue |
F | VAL35 |
F | GLY36 |
F | GLY38 |
F | PHE39 |
F | ALA40 |
F | ASP59 |
F | ARG60 |
F | ARG61 |
F | GLY66 |
F | ASN67 |
F | TYR82 |
F | PRO84 |
F | HIS85 |
F | ILE86 |
F | THR241 |
F | ASP242 |
F | TYR243 |
F | ARG244 |
F | GLY259 |
F | GLU325 |
F | GLY363 |
F | ARG364 |
F | TYR371 |
F | ASN372 |
F | MET373 |
F | VAL376 |
F | HOH404 |
F | HOH408 |
F | GDU500 |
site_id | BC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE GDU F 500 |
Chain | Residue |
F | HIS109 |
F | PHE175 |
F | PHE176 |
F | TYR179 |
F | THR180 |
F | TRP184 |
F | VAL195 |
F | ARG198 |
F | TYR209 |
F | PHE210 |
F | ASN296 |
F | ARG305 |
F | TYR335 |
F | TYR370 |
F | HOH418 |
F | FAD450 |
site_id | BC4 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE GDU G 500 |
Chain | Residue |
G | HIS109 |
G | PHE175 |
G | PHE176 |
G | TYR179 |
G | THR180 |
G | TRP184 |
G | VAL195 |
G | ARG198 |
G | VAL199 |
G | TYR209 |
G | PHE210 |
G | ASN296 |
G | ARG305 |
G | TYR335 |
G | TYR370 |
G | ASN372 |
G | HOH404 |
G | HOH523 |
G | FDA1385 |
site_id | BC5 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE FDA G 1385 |
Chain | Residue |
G | VAL35 |
G | GLY36 |
G | GLY38 |
G | PHE39 |
G | ALA40 |
G | ASP59 |
G | ARG60 |
G | ARG61 |
G | GLY66 |
G | ASN67 |
G | TYR82 |
G | PRO84 |
G | HIS85 |
G | ILE86 |
G | ASP242 |
G | TYR243 |
G | THR258 |
G | GLY259 |
G | LEU277 |
G | TYR334 |
G | GLY363 |
G | ARG364 |
G | TYR371 |
G | ASN372 |
G | MET373 |
G | VAL376 |
G | HOH399 |
G | HOH401 |
G | HOH417 |
G | GDU500 |
site_id | BC6 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE FAD H 450 |
Chain | Residue |
H | VAL35 |
H | GLY36 |
H | GLY38 |
H | PHE39 |
H | ALA40 |
H | ASP59 |
H | ARG60 |
H | ARG61 |
H | GLY66 |
H | ASN67 |
H | TYR82 |
H | PRO84 |
H | HIS85 |
H | ILE86 |
H | HIS88 |
H | THR241 |
H | ASP242 |
H | TYR243 |
H | GLY259 |
H | GLU325 |
H | GLY363 |
H | ARG364 |
H | TYR371 |
H | ASN372 |
H | MET373 |
H | HOH402 |
H | HOH410 |
H | HOH411 |
H | GDU500 |
site_id | BC7 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE GDU H 500 |
Chain | Residue |
H | HIS109 |
H | PHE175 |
H | PHE176 |
H | TYR179 |
H | THR180 |
H | TRP184 |
H | VAL195 |
H | ARG198 |
H | TYR209 |
H | PHE210 |
H | THR294 |
H | ASN296 |
H | ARG305 |
H | TYR335 |
H | TYR370 |
H | HOH419 |
H | FAD450 |
site_id | BC8 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE FAD I 450 |
Chain | Residue |
I | GLY36 |
I | GLY38 |
I | PHE39 |
I | ALA40 |
I | ASP59 |
I | ARG60 |
I | ARG61 |
I | GLY66 |
I | ASN67 |
I | TYR82 |
I | PRO84 |
I | HIS85 |
I | ILE86 |
I | HIS88 |
I | THR241 |
I | ASP242 |
I | TYR243 |
I | GLY259 |
I | GLY363 |
I | ARG364 |
I | TYR371 |
I | ASN372 |
I | MET373 |
I | VAL376 |
I | HOH398 |
I | HOH399 |
I | HOH405 |
I | HOH409 |
I | HOH413 |
I | HOH420 |
I | GDU500 |
site_id | BC9 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE GDU I 500 |
Chain | Residue |
I | HIS109 |
I | PHE175 |
I | PHE176 |
I | TYR179 |
I | THR180 |
I | TRP184 |
I | ARG198 |
I | VAL199 |
I | TYR209 |
I | PHE210 |
I | THR294 |
I | ASN296 |
I | ARG305 |
I | TYR335 |
I | TYR370 |
I | HOH400 |
I | HOH413 |
I | FAD450 |
I | HOH579 |
site_id | CC1 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE FAD J 450 |
Chain | Residue |
J | VAL35 |
J | GLY36 |
J | GLY38 |
J | PHE39 |
J | ALA40 |
J | ASP59 |
J | ARG60 |
J | ARG61 |
J | GLY66 |
J | ASN67 |
J | TYR82 |
J | PRO84 |
J | HIS85 |
J | ILE86 |
J | THR241 |
J | ASP242 |
J | TYR243 |
J | GLY259 |
J | PRO260 |
J | LEU277 |
J | GLU325 |
J | GLY363 |
J | ARG364 |
J | TYR371 |
J | ASN372 |
J | MET373 |
J | VAL376 |
J | HOH399 |
J | HOH423 |
J | GDU500 |
site_id | CC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE GDU J 500 |
Chain | Residue |
J | ILE86 |
J | HIS109 |
J | PHE175 |
J | PHE176 |
J | TYR179 |
J | THR180 |
J | TRP184 |
J | VAL195 |
J | ARG198 |
J | TYR209 |
J | PHE210 |
J | ASN296 |
J | ARG305 |
J | TYR335 |
J | TYR370 |
J | ASN372 |
J | HOH415 |
J | FAD450 |