3NM3
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 | 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 | 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 | 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 | 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 | 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 | 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 | 3 |
Details | BINDING SITE FOR RESIDUE MG A 3001 |
Chain | Residue |
A | ASP76 |
A | ASP95 |
A | POP4001 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 3002 |
Chain | Residue |
B | ASN75 |
B | ASP76 |
B | GLY92 |
B | ASP95 |
B | POP4002 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG C 3003 |
Chain | Residue |
C | ASP95 |
C | POP4003 |
C | ASP76 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG D 3004 |
Chain | Residue |
D | LYS47 |
D | ASP76 |
D | ASP95 |
D | POP4004 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG E 3005 |
Chain | Residue |
E | LYS47 |
E | ASP76 |
E | GLY92 |
E | ASP95 |
E | POP4005 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG F 3006 |
Chain | Residue |
F | ASP76 |
F | ASP95 |
F | POP4006 |
site_id | AC7 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE TPS A 2001 |
Chain | Residue |
A | TYR13 |
A | GLN43 |
A | ARG45 |
A | HIS90 |
A | SER114 |
A | THR143 |
A | THR145 |
A | LYS146 |
A | ILE179 |
A | GLY180 |
A | GLY181 |
A | VAL209 |
A | SER210 |
A | POP4001 |
site_id | AC8 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE TPS B 2002 |
Chain | Residue |
B | TYR13 |
B | GLN43 |
B | ARG45 |
B | HIS90 |
B | THR143 |
B | THR145 |
B | ILE179 |
B | GLY180 |
B | GLY181 |
B | CYS207 |
B | VAL209 |
B | SER210 |
B | POP4002 |
site_id | AC9 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE TPS C 2003 |
Chain | Residue |
C | GLN43 |
C | ARG45 |
C | HIS90 |
C | SER114 |
C | THR143 |
C | THR145 |
C | ILE179 |
C | GLY181 |
C | VAL209 |
C | SER210 |
C | POP4003 |
site_id | BC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE TPS D 2004 |
Chain | Residue |
D | GLN43 |
D | ARG45 |
D | ASN75 |
D | HIS90 |
D | SER114 |
D | THR143 |
D | THR145 |
D | ILE179 |
D | GLY180 |
D | GLY181 |
D | VAL209 |
D | SER210 |
D | POP4004 |
site_id | BC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE TPS E 2005 |
Chain | Residue |
E | GLN43 |
E | ARG45 |
E | ASN75 |
E | HIS90 |
E | SER114 |
E | THR143 |
E | THR145 |
E | ILE179 |
E | GLY180 |
E | GLY181 |
E | VAL209 |
E | SER210 |
E | POP4005 |
site_id | BC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE TPS F 2006 |
Chain | Residue |
F | GLN43 |
F | ARG45 |
F | HIS90 |
F | SER114 |
F | THR143 |
F | THR145 |
F | ILE179 |
F | GLY180 |
F | GLY181 |
F | VAL209 |
F | SER210 |
F | POP4006 |
site_id | BC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE POP A 4001 |
Chain | Residue |
A | ARG45 |
A | LYS47 |
A | ASN75 |
A | ASP76 |
A | GLY92 |
A | ASP95 |
A | SER114 |
A | LYS146 |
A | TPS2001 |
A | MG3001 |
site_id | BC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE POP B 4002 |
Chain | Residue |
B | ARG45 |
B | LYS47 |
B | ASN75 |
B | ASP76 |
B | GLY92 |
B | ASP95 |
B | SER114 |
B | LYS146 |
B | TPS2002 |
B | MG3002 |
site_id | BC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE POP C 4003 |
Chain | Residue |
C | ARG45 |
C | LYS47 |
C | ASN75 |
C | ASP76 |
C | GLY92 |
C | ASP95 |
C | SER114 |
C | TPS2003 |
C | MG3003 |
site_id | BC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE POP D 4004 |
Chain | Residue |
D | ARG45 |
D | LYS47 |
D | ASN75 |
D | ASP76 |
D | GLY92 |
D | SER114 |
D | LYS146 |
D | TPS2004 |
D | MG3004 |
site_id | BC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE POP E 4005 |
Chain | Residue |
E | ARG45 |
E | LYS47 |
E | ASN75 |
E | ASP76 |
E | GLY92 |
E | SER114 |
E | LYS146 |
E | TPS2005 |
E | MG3005 |
site_id | BC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE POP F 4006 |
Chain | Residue |
F | ARG45 |
F | ASN75 |
F | ASP76 |
F | GLY92 |
F | SER114 |
F | TPS2006 |
F | MG3006 |