4S23
Structure of the GcpE-HMBPP complex from Thermus thermophilius
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0016114 | biological_process | terpenoid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| A | 0046429 | molecular_function | 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity (ferredoxin) |
| 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 | 0141197 | molecular_function | 4-hydroxy-3-methylbut-2-enyl-diphosphate synthase activity (flavodoxin) |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0008299 | biological_process | isoprenoid biosynthetic process |
| B | 0016114 | biological_process | terpenoid biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| B | 0046429 | molecular_function | 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity (ferredoxin) |
| 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 | 0141197 | molecular_function | 4-hydroxy-3-methylbut-2-enyl-diphosphate synthase activity (flavodoxin) |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SF4 A 501 |
| Chain | Residue |
| A | CYS297 |
| A | CYS300 |
| A | MET341 |
| A | CYS343 |
| A | HOH852 |
| B | H6P503 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE MES A 502 |
| Chain | Residue |
| A | PRO292 |
| A | GLU293 |
| A | VAL294 |
| A | SER316 |
| A | HOH602 |
| A | HOH616 |
| A | HOH1094 |
| B | LYS238 |
| A | GLU280 |
| A | GLN283 |
| A | ALA291 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE H6P A 503 |
| Chain | Residue |
| A | ARG56 |
| A | ASP87 |
| A | HIS89 |
| A | ARG110 |
| A | ARG141 |
| A | ASN145 |
| A | LYS204 |
| A | THR231 |
| A | ARG260 |
| A | SER262 |
| A | HOH601 |
| A | HOH607 |
| B | ASN346 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SF4 B 501 |
| Chain | Residue |
| A | HOH607 |
| B | CYS297 |
| B | CYS300 |
| B | THR303 |
| B | CYS343 |
| B | HOH912 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MES B 502 |
| Chain | Residue |
| A | LYS238 |
| B | GLU280 |
| B | GLN283 |
| B | ALA291 |
| B | PRO292 |
| B | GLU293 |
| B | VAL294 |
| B | SER316 |
| B | HOH618 |
| B | HOH647 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE H6P B 503 |
| Chain | Residue |
| A | ASN346 |
| A | SF4501 |
| A | HOH852 |
| B | ARG56 |
| B | HIS89 |
| B | ARG110 |
| B | ARG141 |
| B | ASN145 |
| B | LYS204 |
| B | THR231 |
| B | GLU232 |
| B | ARG260 |
| B | SER262 |
| B | HOH636 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
