3NM1
The Crystal Structure of Candida glabrata THI6, a Bifunctional Enzyme involved in Thiamin Biosyhthesis of Eukaryotes
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004417 | molecular_function | hydroxyethylthiazole kinase activity |
A | 0004789 | molecular_function | thiamine-phosphate diphosphorylase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0009228 | biological_process | thiamine biosynthetic process |
A | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004417 | molecular_function | hydroxyethylthiazole kinase activity |
B | 0004789 | molecular_function | thiamine-phosphate diphosphorylase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0009228 | biological_process | thiamine biosynthetic process |
B | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0004417 | molecular_function | hydroxyethylthiazole kinase activity |
C | 0004789 | molecular_function | thiamine-phosphate diphosphorylase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0009228 | biological_process | thiamine biosynthetic process |
C | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
C | 0016740 | molecular_function | transferase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0004417 | molecular_function | hydroxyethylthiazole kinase activity |
D | 0004789 | molecular_function | thiamine-phosphate diphosphorylase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0009228 | biological_process | thiamine biosynthetic process |
D | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
D | 0016740 | molecular_function | transferase activity |
D | 0046872 | molecular_function | metal ion binding |
E | 0000287 | molecular_function | magnesium ion binding |
E | 0004417 | molecular_function | hydroxyethylthiazole kinase activity |
E | 0004789 | molecular_function | thiamine-phosphate diphosphorylase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0005829 | cellular_component | cytosol |
E | 0009228 | biological_process | thiamine biosynthetic process |
E | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
E | 0016740 | molecular_function | transferase activity |
E | 0046872 | molecular_function | metal ion binding |
F | 0000287 | molecular_function | magnesium ion binding |
F | 0004417 | molecular_function | hydroxyethylthiazole kinase activity |
F | 0004789 | molecular_function | thiamine-phosphate diphosphorylase activity |
F | 0005524 | molecular_function | ATP binding |
F | 0005737 | cellular_component | cytoplasm |
F | 0005829 | cellular_component | cytosol |
F | 0009228 | biological_process | thiamine biosynthetic process |
F | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
F | 0016740 | molecular_function | transferase activity |
F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 3NM A 541 |
Chain | Residue |
A | ARG45 |
A | IFP542 |
A | POP543 |
A | GLY138 |
A | THR139 |
A | THR143 |
A | THR145 |
A | LYS151 |
A | GLY181 |
A | VAL209 |
A | SER210 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE IFP A 542 |
Chain | Residue |
A | TYR13 |
A | GLN43 |
A | HIS90 |
A | SER114 |
A | TYR134 |
A | GLY136 |
A | VAL177 |
A | ILE179 |
A | CYS207 |
A | 3NM541 |
A | POP543 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE POP A 543 |
Chain | Residue |
A | ARG45 |
A | LYS47 |
A | ASN75 |
A | ASP76 |
A | GLY92 |
A | ASP95 |
A | SER114 |
A | LYS146 |
A | 3NM541 |
A | IFP542 |
A | MG544 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE 3NM F 541 |
Chain | Residue |
F | ARG45 |
F | GLY138 |
F | THR139 |
F | THR143 |
F | THR145 |
F | LYS146 |
F | LYS151 |
F | GLY180 |
F | GLY181 |
F | VAL209 |
F | SER210 |
F | IFP542 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE IFP F 542 |
Chain | Residue |
F | TYR13 |
F | GLN43 |
F | HIS90 |
F | SER114 |
F | TYR134 |
F | GLY136 |
F | VAL177 |
F | ILE179 |
F | CYS207 |
F | 3NM541 |
F | POP543 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE POP F 543 |
Chain | Residue |
F | ARG45 |
F | LYS47 |
F | ASN75 |
F | ASP76 |
F | GLY92 |
F | ASP95 |
F | SER114 |
F | LYS146 |
F | IFP542 |
F | MG544 |
site_id | AC7 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE 3NM E 541 |
Chain | Residue |
E | ARG45 |
E | GLY138 |
E | THR139 |
E | THR143 |
E | THR145 |
E | LYS151 |
E | ILE179 |
E | GLY181 |
E | VAL209 |
E | SER210 |
E | IFP542 |
E | POP543 |
site_id | AC8 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE IFP E 542 |
Chain | Residue |
E | TYR13 |
E | VAL15 |
E | GLN43 |
E | HIS90 |
E | SER114 |
E | TYR134 |
E | GLY136 |
E | VAL177 |
E | ILE179 |
E | CYS207 |
E | 3NM541 |
E | POP543 |
site_id | AC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE POP E 543 |
Chain | Residue |
E | MG544 |
E | ARG45 |
E | LYS47 |
E | ASN75 |
E | GLY92 |
E | ASP95 |
E | SER114 |
E | LYS146 |
E | 3NM541 |
E | IFP542 |
site_id | BC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 3NM D 541 |
Chain | Residue |
D | ARG45 |
D | THR139 |
D | THR143 |
D | THR145 |
D | LYS146 |
D | LYS151 |
D | GLY180 |
D | GLY181 |
D | VAL209 |
D | SER210 |
D | IFP542 |
site_id | BC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE IFP D 542 |
Chain | Residue |
D | TYR13 |
D | VAL15 |
D | GLN43 |
D | HIS90 |
D | SER114 |
D | TYR134 |
D | GLY136 |
D | VAL177 |
D | ILE179 |
D | CYS207 |
D | 3NM541 |
D | POP543 |
site_id | BC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE POP D 543 |
Chain | Residue |
D | ARG45 |
D | LYS47 |
D | ASN75 |
D | ASP76 |
D | GLY92 |
D | ASP95 |
D | SER114 |
D | LYS146 |
D | IFP542 |
D | MG544 |
site_id | BC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE 3NM C 541 |
Chain | Residue |
C | ARG45 |
C | GLY138 |
C | THR139 |
C | THR143 |
C | THR145 |
C | LYS151 |
C | ILE179 |
C | GLY181 |
C | VAL209 |
C | SER210 |
C | IFP542 |
C | POP543 |
site_id | BC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE IFP C 542 |
Chain | Residue |
C | TYR13 |
C | VAL15 |
C | GLN43 |
C | HIS90 |
C | SER114 |
C | TYR134 |
C | GLY136 |
C | VAL177 |
C | ILE179 |
C | CYS207 |
C | 3NM541 |
C | POP543 |
site_id | BC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE POP C 543 |
Chain | Residue |
C | ARG45 |
C | LYS47 |
C | ASN75 |
C | ASP76 |
C | GLY92 |
C | ASP95 |
C | SER114 |
C | LYS146 |
C | 3NM541 |
C | IFP542 |
C | MG544 |
site_id | BC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 3NM B 541 |
Chain | Residue |
B | ARG45 |
B | GLY138 |
B | THR139 |
B | THR143 |
B | THR145 |
B | LYS151 |
B | ILE179 |
B | GLY181 |
B | VAL209 |
B | SER210 |
B | IFP542 |
site_id | BC8 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE IFP B 542 |
Chain | Residue |
B | TYR13 |
B | VAL15 |
B | GLN43 |
B | ASN75 |
B | HIS90 |
B | SER114 |
B | TYR134 |
B | GLY136 |
B | VAL177 |
B | ILE179 |
B | CYS207 |
B | 3NM541 |
B | POP543 |
site_id | BC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE POP B 543 |
Chain | Residue |
B | ARG45 |
B | LYS47 |
B | ASN75 |
B | GLY92 |
B | ASP95 |
B | SER114 |
B | LYS146 |
B | IFP542 |
B | MG544 |
site_id | CC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 544 |
Chain | Residue |
A | ASP76 |
A | ASP95 |
A | POP543 |
site_id | CC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG F 544 |
Chain | Residue |
F | ASP76 |
F | ASP95 |
F | POP543 |
site_id | CC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG E 544 |
Chain | Residue |
E | LYS47 |
E | ASP76 |
E | ASP95 |
E | POP543 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 544 |
Chain | Residue |
D | ASN75 |
D | ASP76 |
D | GLY92 |
D | ASP95 |
D | POP543 |
site_id | CC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG C 544 |
Chain | Residue |
C | LYS47 |
C | ASP76 |
C | ASP95 |
C | POP543 |
site_id | CC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 544 |
Chain | Residue |
B | LYS47 |
B | ASN75 |
B | ASP76 |
B | ASP95 |
B | POP543 |