3EPN
Crystal structure of Caulobacter crescentus ThiC complexed with imidazole ribonucleotide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009228 | biological_process | thiamine biosynthetic process |
| A | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016830 | molecular_function | carbon-carbon lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| A | 0070284 | molecular_function | 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009228 | biological_process | thiamine biosynthetic process |
| B | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016830 | molecular_function | carbon-carbon lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0070284 | molecular_function | 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE IRN A1001 |
| Chain | Residue |
| A | ASN219 |
| A | GLU413 |
| A | GLY414 |
| A | TYR440 |
| A | MET248 |
| A | TYR277 |
| A | HIS313 |
| A | SER333 |
| A | ARG334 |
| A | GLY335 |
| A | ASP374 |
| A | ARG377 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE IRN A1002 |
| Chain | Residue |
| B | ASN219 |
| B | MET248 |
| B | TYR277 |
| B | HIS313 |
| B | SER333 |
| B | ARG334 |
| B | GLY335 |
| B | ASP374 |
| B | ARG377 |
| B | GLU413 |
| B | GLY414 |
| B | TYR440 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18953358, ECO:0007744|PDB:3EPN |
| Chain | Residue | Details |
| A | SER333 | |
| A | ASP374 | |
| A | GLU413 | |
| A | TYR440 | |
| B | ASN219 | |
| B | MET248 | |
| B | TYR277 | |
| B | HIS313 | |
| B | SER333 | |
| B | ASP374 | |
| B | GLU413 | |
| B | TYR440 | |
| A | ASN219 | |
| A | MET248 | |
| A | TYR277 | |
| A | HIS313 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18953358, ECO:0007744|PDB:3EPM |
| Chain | Residue | Details |
| A | HIS417 | |
| A | HIS481 | |
| B | HIS417 | |
| B | HIS481 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25813242, ECO:0007744|PDB:4S2A |
| Chain | Residue | Details |
| A | CYS561 | |
| A | CYS564 | |
| A | CYS569 | |
| B | CYS561 | |
| B | CYS564 | |
| B | CYS569 |
