1AG9
FLAVODOXINS THAT ARE REQUIRED FOR ENZYME ACTIVATION: THE STRUCTURE OF OXIDIZED FLAVODOXIN FROM ESCHERICHIA COLI AT 1.8 ANGSTROMS RESOLUTION.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0010181 | molecular_function | FMN binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0010181 | molecular_function | FMN binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 200 |
| Chain | Residue |
| A | TYR59 |
| A | GLU61 |
| A | HOH406 |
| A | HOH407 |
| B | ASP67 |
| B | HOH1001 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 1000 |
| Chain | Residue |
| A | HOH408 |
| B | TYR59 |
| B | GLU61 |
| B | HOH1002 |
| B | HOH1003 |
| A | ASP67 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA B 300 |
| Chain | Residue |
| B | BTB301 |
| B | HOH1004 |
| B | HOH1005 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 350 |
| Chain | Residue |
| A | BTB351 |
| A | HOH409 |
| A | HOH410 |
| A | HOH411 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 404 |
| Chain | Residue |
| A | HOH474 |
| B | ALA62 |
| B | HOH1053 |
| B | HOH1073 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 405 |
| Chain | Residue |
| A | ALA62 |
| A | HOH422 |
| A | HOH512 |
| A | HOH538 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 400 |
| Chain | Residue |
| A | GLU61 |
| A | HOH474 |
| A | HOH512 |
| B | ASP67 |
| B | HOH1116 |
| B | HOH1129 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 401 |
| Chain | Residue |
| A | ASP67 |
| A | HOH484 |
| B | GLU61 |
| B | HOH1052 |
| B | HOH1074 |
| B | HOH1151 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA B 402 |
| Chain | Residue |
| B | ASP43 |
| B | GLU96 |
| B | HOH1070 |
| B | HOH1075 |
| B | HOH1076 |
| B | HOH1085 |
| B | HOH1158 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 403 |
| Chain | Residue |
| B | ALA46 |
| B | HOH1071 |
| B | HOH1091 |
| B | HOH1152 |
| B | HOH1156 |
| B | HOH1167 |
| site_id | BC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FMN A 177 |
| Chain | Residue |
| A | SER10 |
| A | ASP11 |
| A | THR12 |
| A | GLY13 |
| A | ASN14 |
| A | THR15 |
| A | PRO55 |
| A | THR56 |
| A | TRP57 |
| A | TYR58 |
| A | TYR59 |
| A | GLY60 |
| A | CYS88 |
| A | GLY89 |
| A | ASP90 |
| A | TYR94 |
| A | TYR97 |
| A | PHE98 |
| A | CYS99 |
| A | ASP147 |
| A | HOH440 |
| A | HOH446 |
| site_id | BC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FMN B 177 |
| Chain | Residue |
| B | SER10 |
| B | ASP11 |
| B | THR12 |
| B | GLY13 |
| B | ASN14 |
| B | THR15 |
| B | PRO55 |
| B | THR56 |
| B | TRP57 |
| B | TYR58 |
| B | TYR59 |
| B | GLY60 |
| B | CYS88 |
| B | GLY89 |
| B | ASP90 |
| B | TYR94 |
| B | TYR97 |
| B | PHE98 |
| B | CYS99 |
| B | ASP147 |
| B | HOH1006 |
| B | HOH1028 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BTB B 301 |
| Chain | Residue |
| B | GLU151 |
| B | CA300 |
| B | HOH1004 |
| B | HOH1005 |
| B | HOH1162 |
| B | ARG148 |
| site_id | BC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE BTB A 351 |
| Chain | Residue |
| A | ASN17 |
| A | GLU146 |
| A | CA350 |
| A | HOH409 |
| A | HOH410 |
| A | HOH411 |
| A | HOH471 |
| A | HOH475 |
| B | SER10 |
| B | ASP11 |
| B | GLY13 |
| B | GLU16 |
| B | HOH1032 |
| B | HOH1041 |
| site_id | FMA |
| Number of Residues | 1 |
| Details | FMN BINDING SITE. |
| Chain | Residue |
| A | FMN177 |
| site_id | FMB |
| Number of Residues | 1 |
| Details | FMN BINDING SITE. |
| Chain | Residue |
| B | FMN177 |
Functional Information from PROSITE/UniProt
| site_id | PS00201 |
| Number of Residues | 17 |
| Details | FLAVODOXIN Flavodoxin signature. IFFgSDtGnTEniAKmI |
| Chain | Residue | Details |
| A | ILE6-ILE22 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 322 |
| Details | Domain: {"description":"Flavodoxin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00088","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1AG9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1AHN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2MOK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1AG9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1AHN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
