2ZXI
Structure of Aquifex aeolicus GidA in the form II crystal
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002098 | biological_process | tRNA wobble uridine modification |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008033 | biological_process | tRNA processing |
| A | 0030488 | biological_process | tRNA methylation |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0002098 | biological_process | tRNA wobble uridine modification |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008033 | biological_process | tRNA processing |
| B | 0030488 | biological_process | tRNA methylation |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0002098 | biological_process | tRNA wobble uridine modification |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0008033 | biological_process | tRNA processing |
| C | 0030488 | biological_process | tRNA methylation |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0002098 | biological_process | tRNA wobble uridine modification |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0008033 | biological_process | tRNA processing |
| D | 0030488 | biological_process | tRNA methylation |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE FAD A 618 |
| Chain | Residue |
| A | ILE13 |
| A | CYS48 |
| A | LYS57 |
| A | GLU124 |
| A | GLU125 |
| A | VAL126 |
| A | THR155 |
| A | THR156 |
| A | GLY157 |
| A | THR158 |
| A | PHE159 |
| A | GLY14 |
| A | SER181 |
| A | THR200 |
| A | GLY201 |
| A | TYR348 |
| A | ILE350 |
| A | GLY376 |
| A | ASN377 |
| A | THR382 |
| A | GLY383 |
| A | ALA387 |
| A | GLY15 |
| A | ARG434 |
| A | HOH619 |
| A | HOH623 |
| A | HOH626 |
| A | HOH635 |
| A | HOH655 |
| A | HOH659 |
| A | HOH665 |
| A | HOH672 |
| A | HOH713 |
| A | GLY16 |
| A | HIS17 |
| A | ALA18 |
| A | PHE36 |
| A | VAL37 |
| A | LEU38 |
| site_id | AC2 |
| Number of Residues | 42 |
| Details | BINDING SITE FOR RESIDUE FAD B 618 |
| Chain | Residue |
| B | ILE13 |
| B | GLY14 |
| B | GLY15 |
| B | GLY16 |
| B | HIS17 |
| B | ALA18 |
| B | VAL37 |
| B | LEU38 |
| B | CYS48 |
| B | LYS57 |
| B | GLU124 |
| B | GLU125 |
| B | VAL126 |
| B | THR155 |
| B | THR156 |
| B | GLY157 |
| B | THR158 |
| B | PHE159 |
| B | ARG175 |
| B | SER181 |
| B | THR200 |
| B | GLY201 |
| B | TYR348 |
| B | ILE350 |
| B | GLY376 |
| B | ASN377 |
| B | THR382 |
| B | GLY383 |
| B | TYR384 |
| B | ALA387 |
| B | ARG434 |
| B | HOH620 |
| B | HOH621 |
| B | HOH628 |
| B | HOH637 |
| B | HOH640 |
| B | HOH647 |
| B | HOH649 |
| B | HOH675 |
| B | HOH698 |
| B | HOH850 |
| B | HOH907 |
| site_id | AC3 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE FAD C 618 |
| Chain | Residue |
| C | ARG175 |
| C | SER181 |
| C | THR200 |
| C | GLY201 |
| C | TYR348 |
| C | ILE350 |
| C | GLY376 |
| C | ASN377 |
| C | THR382 |
| C | GLY383 |
| C | TYR384 |
| C | ALA387 |
| C | ARG434 |
| C | HOH619 |
| C | HOH620 |
| C | HOH622 |
| C | HOH626 |
| C | HOH628 |
| C | HOH644 |
| C | HOH649 |
| C | HOH653 |
| C | HOH654 |
| C | ILE13 |
| C | GLY14 |
| C | GLY15 |
| C | GLY16 |
| C | HIS17 |
| C | ALA18 |
| C | VAL37 |
| C | LEU38 |
| C | CYS48 |
| C | LYS57 |
| C | GLU124 |
| C | GLU125 |
| C | VAL126 |
| C | THR155 |
| C | THR156 |
| C | GLY157 |
| C | THR158 |
| C | PHE159 |
| site_id | AC4 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE FAD D 618 |
| Chain | Residue |
| D | ILE13 |
| D | GLY14 |
| D | GLY15 |
| D | GLY16 |
| D | HIS17 |
| D | ALA18 |
| D | PHE36 |
| D | VAL37 |
| D | LEU38 |
| D | CYS48 |
| D | LYS57 |
| D | GLU124 |
| D | GLU125 |
| D | VAL126 |
| D | THR155 |
| D | THR156 |
| D | GLY157 |
| D | THR158 |
| D | PHE159 |
| D | SER181 |
| D | THR200 |
| D | GLY201 |
| D | TYR348 |
| D | ILE350 |
| D | GLY376 |
| D | ASN377 |
| D | THR382 |
| D | GLY383 |
| D | ALA387 |
| D | ARG434 |
| D | HOH620 |
| D | HOH624 |
| D | HOH625 |
| D | HOH637 |
| D | HOH649 |
| D | HOH651 |
| D | HOH680 |
| D | HOH689 |
| D | HOH708 |
| D | HOH763 |
Functional Information from PROSITE/UniProt
| site_id | PS01280 |
| Number of Residues | 15 |
| Details | GIDA_1 Glucose inhibited division protein A family signature 1. GPrYCPSIEdKIvKF |
| Chain | Residue | Details |
| A | GLY280-PHE294 |
| site_id | PS01281 |
| Number of Residues | 24 |
| Details | GIDA_2 Glucose inhibited division protein A family signature 2. AGNfNGttGYeEAAGQGIVAGINA |
| Chain | Residue | Details |
| A | ALA375-ALA398 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2008","submissionDatabase":"PDB data bank","title":"Crystal structure of gidA from Aquifex aeolicus.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}}]} |
| Chain | Residue | Details |
